Serum enzymes

References

• Abderhalden R. Clinical Enzymology, P. Oesper. Van Nostrand, Princeton, NJ 1961
   Google Scholar
• Wilkinson J. H. An Introduction to Diagnostic Enzymology. Edward Arnold, London 1962
   Google Scholar
• Hess B. Enzymes in Blood Plasma. Academic Press, New York 1963
   Google Scholar
• Henley K. S., Schmidt E., Schmidt F. W. Enzymes in Serum: Their Use in Diagnosis. Charles C Thomas, Springfield, Ill 1966
   Google Scholar
• Batsakis J. G., Briere R. O. Interpretive Enzymology. Charles C Thomas, Springfield, Ill 1967
   Google Scholar
• Latner A. L., Skillen A. W. Isoenzymes in Biology and Medicine. Academic Press, London 1968
   Google Scholar
• Wilkinson J. H. Isoenzymes, 2nd ed. Methuen, London 1970
   Google Scholar
• Nydick I., Wróblewski F., La Due J. S. Evidence for increased serum glutamic oxalacetic transaminase (SGO‐T) activity following graded myocardial infarcts in dogs. Circulation 1955; 12: 161
   PubMed Web of Science ®Google Scholar
• Bruns F., Neuhaus J. Glycolytic serum and liver enzyme activities in experimental liver damage. Arch. Biochem. Biophys. 1955; 55: 588
   Web of Science ®Google Scholar
• Hess B., Gehm E. Über die Milchsäuredehydrogenase im menschlichen Serum. Klin. Wschr. 1955; 33: 91
   PubMedGoogle Scholar
• Thomson W. H. S., Leyburn P., Walton J. N. Serum enzyme activity in muscular dystrophy. Brit. Med. J. 1960; 5208: 1276
   Google Scholar
• LaDue J. S., Wróblewski F., Karmen A. Serum glutamic oxaloacetic transaminase activity in human acute transmural myocardial infarction. Science 1954; 120: 497
   PubMed Web of Science ®Google Scholar
• DeRitis F., Coltorti M., Giusti G. Attività transaminasica del siero umano nell'epatite virale. Minerva Med. 1955; 46: 1207
   PubMedGoogle Scholar
• Henley K. S., Schmidt E., Schmidt F. W. Serum enzymes. J.A.M.A. 1960; 174: 977
   PubMed Web of Science ®Google Scholar
• Zierler K. L. Increased muscle permeability to aldolase produced by depolarization and by metabolic inhibitors. Amer. J. Physiol. 1958; 193: 534
   PubMed Web of Science ®Google Scholar
• Wu R. Leakage of enzymes from ascites tumor cells. Cancer Res. 1959; 19: 1217
   PubMedGoogle Scholar
• Henley K. S., Sorensen O., Pollard H. M. Some enzymatic properties of suspensions of parenchymatous liver cells. Nature 1959; 184: 140
   Google Scholar
• Schmidt E., Schmidt F. W., Herfarth C. Studien zum Austritt von Zell‐Enzymen am Modell der isolierten, perfundierten Rattenleber. Enzym. Biol. Clin. 1966; 7: 53
   PubMedGoogle Scholar
• Engelhardt‐Goekel A., Loebel R., Seitz W., Woller I. Über das Verhalten und die herkunft glykolytischer Serumenzyme beim menschen und ihre diagnostische Bedeutung. Klin. Wschr. 1958; 36: 462
   PubMedGoogle Scholar
• Schmidt F. W. Enzymbestimmungen zur Diagnose und Verlaufsbeobachtung von Lebererkrankungen. Vehr. Deutsch. Ges. Inn. Med. 1964; 70: 612
   PubMedGoogle Scholar
• Wróblewski F., LaDue J. S. Serum glutamic pyruvic transaminase in cardiac and hepatic disease. Proc. Soc. Exp. Biol. Med. 1956; 91: 569
   PubMed Web of Science ®Google Scholar
• Henry R. J., Chiamori N., Golub O. J., Berkman S. Revised spectrophotometric methods for the determination of glutamic‐oxalacetic transaminase, glutamic‐pyruvic transaminase, and lactic acid dehydrogenase. Amer. J. Clin. Path. 1960; 30: 149
   Google Scholar
• Arvan D. A., Coyle M. Serum and tissue alanine aminotransferase (GPT) based on optimal substrate concentration. Clin. Chem. 1969; 15: 785
   Google Scholar
• Arvan D. A., Coyle M., Wilkinson J. H., in preparation
   Google Scholar
• Fritz P. J., Vesell E. S., White E. L., Pruitt K. M. The roles of synthesis and degradation in determining tissue concentrations of lactate dehydrogenase – 5. Proc. Nat. Acad. Sci. 1969; 62: 558
   PubMedGoogle Scholar
• Elliott B. A., Wilkinson J. H. The relative efficiencies of some serum enzyme tests in the diagnosis of myocardial infarction. Lancet 1962; 2: 71
   Google Scholar
• Schmidt E., Schmidt F. W. Über Änderungen der Substrat‐Affinität von Malat‐Dehydrogenasen. Klin. Wschr. 1960; 38: 810
   PubMedGoogle Scholar
• Wakim K. G., Fleisher G. A. The fate of enzymes in body fluids—an experimental study. II. Disappearance rates of glutamic‐oxalacetic transaminase I under various conditions. J. Lab. Clin. Med. 1963; 61: 86
   PubMedGoogle Scholar
• Gutman A. B. Serum alkaline phosphatase activity in diseases of the skeletal and hepatobiliary systems. Amer. J. Med. 1959; 27: 875
   PubMed Web of Science ®Google Scholar
• Clubb J. S., Neale F. C., Posen S. The behavior of infused placental alkaline phosphatase in human subjects. J. Lab. Clin. Med. 1965; 66: 493
   PubMed Web of Science ®Google Scholar
• Linde S. On the mechanism of the elevation of serum glutamic‐oxalacetic transaminase (SGOT) in obstructive jaundice. Scand. J. Clin. Lab. Invest. 1958; 10: 308
   PubMedGoogle Scholar
• Lorentz K. Untersuchung von Enzymakitivitäten in der Blasengalle. Klin. Wschr. 1963; 41: 18
   Google Scholar
• Rosalki S. B., Wilkinson J. H. Urinary lactic dehydrogenase in renal disease. Lancet 1959; 2: 327
   PubMedGoogle Scholar
• Strandjord P. E., Thomas K. E., White L. P. Studies on isocitric and lactic dehydrogenases in experimental myocardial infarction. J. Clin. Invest. 1959; 38: 2111
   PubMedGoogle Scholar
• West M., Zimmerman H. J. Serum enzymes in disease. IV. Lactic dehydrogenase and glutamic oxalacetic transaminase levels in renal disease. J. Lab. Clin. Med. 1958; 52: 185
   PubMedGoogle Scholar
• Fleisher G. A., Wakim K. G. The fate of enzymes in body fluids—an experimental study. I. Disappearance rates of glutamic‐pyruvic transaminase under various conditions. J. Lab. Clin. Med. 1963; 61: 76
   PubMedGoogle Scholar
• Fleisher G. A., Wakim K. G. The fate of enzymes in body fluids—an experimental study. III. Disappearance rates of glutamic‐oxalacetic transaminase II under various conditions. J. Lab. Clin. Med. 1963; 61: 98
   Google Scholar
• Wakim K. G., Fleisher G. A. The fate of enzymes in body fluids—an experimental study. IV. Relationships of the reticuloendothelial system to activities and disappearance rates of various enzymes. J. Lab. Clin. Med. 1963; 61: 107
   PubMedGoogle Scholar
• Kutscher W., Wolbergs H. Prostataphosphatase. Z. Physiol. Chem. 1935; 236: 237
   Google Scholar
• Warburg O., Minami S. Versuche an überlebendem Carcimomgewebe. Klin. Wschr. 1923; 2: 776
   Google Scholar
• Bruns F. H., Jacob W. Studien über Serumenzyme bei Erkrankungen der Leber. Die Aktivität der Phosphohexoseisomerase, Aldolase und Alkalischen Phosphatase. Klin. Wschr. 1954; 32: 1041
   PubMedGoogle Scholar
• Bodansky O. Serum phosphohexose isomerase in cancer. II. Comparison with serum phosphoglucomutase activity in metastatic cancer. Cancer 1957; 10: 865
   PubMedGoogle Scholar
• Mahy B. W. J., Rowson K. E. K. Isoenzymic specificity of impaired clearance in mice infected with Riley virus. Science 1965; 149: 756
   PubMedGoogle Scholar
• Hill B. R., Levi C. Elevation of serum component in neoplastic disease. Cancer Res. 1954; 14: 513
   PubMed Web of Science ®Google Scholar
• Zimmerman H. J., Weinstein H. G. Lactic dehydrogenase activity in human serum. J. Lab. Clin. Med. 1956; 48: 607
   PubMedGoogle Scholar
• Blanchaer M. C., Green P. T., Maclean J. P., Hollenberg M. J. Plasma lactic dehydrogenase and phosphohexose isomerase in leukemia. Blood 1958; 13: 245
   PubMedGoogle Scholar
• Magill G. B., Wróblewski F., LaDue J. S. Serum lactic dehydrogenase and serum transaminase in human leukemia. Blood 1959; 14: 870
   PubMed Web of Science ®Google Scholar
• Merten R., Solbach H. G. Enzym‐Verteilungsmuster des glycolytischen Systems und Citronensäurezyklus im Plasma Krebskranker. Klin. Wschr. 1961; 39: 222
   PubMedGoogle Scholar
• West M., Schwartz M. A., Walsh W. C., Zimmerman H. J. Serum enzymes in disease. XI. Glycolytic and oxidative enzymes and transaminases in patients with cancer of the lung. Cancer 1962; 15: 931
   PubMed Web of Science ®Google Scholar
• Wieme R. J., Van Hove W. Z., Van der Straeten M. E. The influence of cytostatic treatment on serum LDH patterns of patients with bronchial carcinoma and its relation to tumor regression. Ann. N.Y. Acad. Sci. 1968; 151: 213
   PubMed Web of Science ®Google Scholar
• Pfleiderer G., Wachsmuth E. D. Alters‐ und functionsabhängige Differenzierung der Lactat‐Dehydrogenasen menschlicher Organe. Biochem. Z. 1961; 334: 185
   PubMedGoogle Scholar
• Richterich R., Burger A. Lactic dehydrogenase isoenzymes in human cancer cells and malignant effusions. Enzym. Biol. Clin. 1963; 3: 65
   Google Scholar
• Barnett H., Gibson A. Lactate dehydrogenase (L.D.H.) isoenzyme patterns in carcinomas of the breast. J. Clin. Path. 1964; 17: 201
   Web of Science ®Google Scholar
• Goldman R. D., Kaplan N. O., Hall T. C. Lactic dehydrogenase in human neoplastic tissues. Cancer Res. 1964; 24: 389
   PubMed Web of Science ®Google Scholar
• Yasin R., Bergel F. Lactate dehydrogenase isoenzyme patterns in human normal and malignant gastric mucosa. Europ. J. Cancer 1965; 1: 203
   Google Scholar
• Poznanska‐Linde H., Wilkinson J. H., Withycombe W. A. Lactate dehydrogenase isoenzymes in malignant tissues. Nature 1966; 209: 727
   PubMedGoogle Scholar
• Langvad E. Lactate dehydrogenase isoenzyme patterns in the tumour‐bearing colon. Int. J. Cancer 1968; 3: 17
   PubMed Web of Science ®Google Scholar
• Langvad E. Lactate dehydrogenase isoenzyme patterns in bronchogenic carcinoma. Europ. J. Cancer 1968; 4: 107
   Google Scholar
• Stagg B. H., Whyley G. A. Some characteristics of lactate dehydrogenase isoenzymes in tumours of the female genital tract. Clin. Chim. Acta 1968; 22: 521
   PubMed Web of Science ®Google Scholar
• Cahn R. D., Kaplan N. O., Levine L., Zwilling E. Nature and development of lactic dehydrogenases. Science 1962; 136: 962
   PubMed Web of Science ®Google Scholar
• Goodfriend T. L., Sokol D. M., Kaplan N. O. Control of synthesis of lactic acid dehydrogenases. J. Molec. Biol. 1966; 15: 18
   PubMed Web of Science ®Google Scholar
• Beautyman W. Dehydrogenase isoenzymes. Lancet 1962; 2: 305
   Google Scholar
• Latner A. L. The dehydrogenase isoenzymes. Proc. Ass. Clin. Biochem. 1964; 3: 120
   Google Scholar
• Fujimoto Y., Nazarian I., Wilkinson J. H. Lactate dehydrogenase isoenzyme polymorphism in a patient with secondary carcinoma of the liver. Enzym. Biol. Clin. 1968; 9: 124
   PubMedGoogle Scholar
• Fishman W. H., Ghosh N. K. Isoenzymes of human alkaline phosphatase. Adv. Clin. Chem. 1967; 10: 255
   Google Scholar
• Bodansky A. Phosphatase studies; determination of serum phosphatase. Factors influencing the accuracy of the determination. J. Biol. Chem. 1933; 101: 93
   Google Scholar
• King E. J., Armstrong A. R. Convenient method for determining serum and bile phosphatase activity. Canad. Med. Ass. J. 1934; 31: 376
   PubMedGoogle Scholar
• Rathbun J. C. Hypophosphatasia. New developmental anomaly. Amer. J. Dis. Child. 1948; 75: 822
   PubMedGoogle Scholar
• Cusworth D. C. The isolation and identification of phosphoethanolamine from the urine of a case of hypophosphatasia. Biochem. J. 1958; 68: 262
   PubMedGoogle Scholar
• Cox R. P., Griffin M. J. Pyrophosphatase activity of mammalian alkaline phosphatase. Lancet 1965; 2: 1018
   Google Scholar
• Fernley H. N., Walker P. G. The substrate specificity of calf‐intestinal alkaline phosphatase. Biochem. J. 1966; 99: 39P
   Google Scholar
• Moss D. W., Eaton R. H., Smith J. K., Whitby L. G. Association of inorganic‐pyrophosphatase activity with human alkaline phosphatase preparations. Biochem. J. 1967; 102: 53
   PubMed Web of Science ®Google Scholar
• Eaton R. H., Moss D. W. Alkaline orthophosphatase and inorganic pyrophosphatase activities in human serum. Nature 1967; 214: 842
   PubMedGoogle Scholar
• Nisselbaum J. S., Schlamowitz M., Bodansky O. Immunochemical studies of functionally similar enzymes. Ann. N.Y. Acad. Sci. 1961; 94: 970
   PubMedGoogle Scholar
• Roche J., Sarles H. Specificité d'organe des phosphatases alcalines et hyperphosphatasémies. Bull. Soc. Chim. Biol. 1951; 33: 667
   PubMedGoogle Scholar
• Sarles H. Sur la phosphomonoestèrase alcaline du sérum et sa caracterisation au moyen de sa constante d'affinité. Compt. Rend. Soc. Biol. 1953; 147: 1688
   PubMedGoogle Scholar
• Moss D. W., Campbell D. M., Anagnostou‐Kakaras E., King E. J. Characterization of tissue alkaline phosphatases and their partial purification by starch‐gel electrophoresis. Biochem. J. 1961; 81: 441
   PubMed Web of Science ®Google Scholar
• Moss D. W., Campbell D. M., Anagnostou‐Kakaras E., King E. J. Separation and Characterization of alkaline phosphatase isoenzymes from blood and other tissues. Pure Appl. Chem. 1961; 3: 397
   Google Scholar
• Dixon T. F., Purdom M. Serum 5'‐nucleotidase. J. Clin. Path. 1954; 7: 341
   PubMed Web of Science ®Google Scholar
• Young I. I. Serum 5‐nucleotidase: Characterization and evaluation in disease states. Ann. N.Y. Acad. Sci. 1958; 75: 357
   PubMedGoogle Scholar
• Eaton R. H., Moss D. W. Action of purified alkaline phosphatases from human liver and small intestine on nucleoside phosphates. Biochem. J. 1967; 104: 65P
   Google Scholar
• Fishman W. H., Green S., Inglis N. I. L‐Phenylalanine: An organ specific, stereospecific inhibitor of human intestinal alkaline phosphatase. Nature 1963; 198: 685
   PubMed Web of Science ®Google Scholar
• Ghosh N. K., Fishman W. H. Characterization of human placental alkaline phosphatase isoenzymes. Fed. Proc. 1967; 26: 558
   Google Scholar
• Fishman W. H., Green S. Automated differential isoenzyme analysis. I. L‐Phenylalanine‐sensitive isoenzymes of human serum alkaline phosphatase. Enzymologia 1967; 33: 89
   Google Scholar
• Fishman W. H., Ghosh N. K. Influence of reagents reacting with metal, thiol and amino sites on catalytic activity and L‐phenylalanine inhibition of rat intestinal alkaline phosphatase. Biochem. J. 1967; 105: 1163
   PubMed Web of Science ®Google Scholar
• Ghosh N. K., Fishman W. H. On the mechanism of inhibition of intestinal alkaline phosphatase by L‐phenylalanine. I. Kinetic studies. J. Biol. Chem. 1966; 241: 2516
   PubMed Web of Science ®Google Scholar
• Bodansky O. Are the phosphatases of bone, kidney, intestine and serum identical? The use of bile acids in their differentiation. J. Biol. Chem. 1937; 118: 341
   Google Scholar
• Bodansky O. The inhibitory effects of dL‐alanine, L‐glutamic acid, L‐lysine and L‐histidine on the activity of intestinal, bone and kidney phosphatases. J. Biol. Chem. 1948; 174: 465
   PubMedGoogle Scholar
• Fishman W. H., Green S., Inglis N. I. Organ‐specific behavior exhibited by rat intestine and liver alkaline phosphatase. Biochim. Biophys. Acta 1962; 62: 363
   PubMed Web of Science ®Google Scholar
• Butterworth P. J., Moss D. W. Action of neuraminidase on human kidney alkaline phosphatase. Nature 1966; 209: 805
   PubMed Web of Science ®Google Scholar
• Birkett D. J., Conyers R. A. J., Neale F. C., Posen S., Brudenell‐Woods J. Action of urea on human alkaline phosphatases: with a description of some automated techniques for the study of enzyme kinetics. Arch. Biochem. 1967; 121: 470
   PubMed Web of Science ®Google Scholar
• Bahr M., Wilkinson J. H. Urea as a selective inhibitor of human tissue alkaline phosphatases. Clin. Chim. Acta 1967; 17: 367
   PubMed Web of Science ®Google Scholar
• Horne M., Cornish C. J., Posen S. Use of urea denaturation in the identification of human alkaline phosphatases. J. Lab. Clin. Med. 1968; 72: 905
   PubMed Web of Science ®Google Scholar
• Vallee B. L. The Enzymes, 2nd ed., P. D. Boyer, H. Lardy, K. Myrback. Academic Press, New York 1960; Vol. 3: 225, part B
   Google Scholar
• Boman H. G., Westlund L. E. Protein chromatography on an anion‐exchange resin. Arch. Biochem. Biophys. 1956; 64: 217
   PubMedGoogle Scholar
• Moss D. W. Heterogeneity of human intestinal alkaline phosphatase. Nature 1963; 200: 1206
   PubMedGoogle Scholar
• Baker R. W. R., Pellegrino C. The separation and detection of serum enzymes by paper electrophoresis. Scand. J. Clin. Lab. Invest. 1954; 6: 94
   PubMed Web of Science ®Google Scholar
• Wolfson W. Q. Location of alpha‐2 globulin by demonstration of alkaline phosphatase during paper electrophoresis. Nature 1957; 180: 550
   PubMedGoogle Scholar
• Haije W. G., de Jong M. Iso‐enzyme patterns of serum alkaline phosphatase in agar‐gel electrophoresis and their clinical significance. Clin. Chim. Acta 1963; 8: 620
   PubMed Web of Science ®Google Scholar
• Korner N. H. Distribution of alkaline phosphatase in serum protein fractions. J. Clin. Path. 1962; 15: 195
   PubMed Web of Science ®Google Scholar
• Posen S., Neale F. C., Clubb J. S. Heat inactivation in the study of human alkaline phosphatases. Ann. Intern. Med. 1965; 62: 1234
   PubMed Web of Science ®Google Scholar
• Inglis N. I., Ghosh N. K., Fishman W. H. Sephadex G‐200 gel electrophoresis of human serum alkaline phosphatase. Anal. Biochem. 1967; 22: 382
   Google Scholar
• Epstein E., Wolf P. I., Horwitz J. P., Zak B. An indigogenic reaction for alkaline phosphatase in disk electrophoresis. Amer. J. Clin. Path. 1967; 48: 530
   PubMedGoogle Scholar
• Smith J. K., Moss D. W. Preparative polyacrylamide gel electrophoresis in the study of isoenzymes. Biochem. J. 1968; 109: 44P
   Google Scholar
• Boyer S. H. Alkaline phosphatase in human sera and placentae. Science 1961; 134: 1002
   PubMed Web of Science ®Google Scholar
• Hodson A. W., Latner A. L., Raine L. Isoenzymes of alkaline phosphatase. Clin. Chim. Acta 1962; 7: 255
   PubMed Web of Science ®Google Scholar
• Taswell H. F., Jeffers D. M. Isoenzymes of serum alkaline phosphatase in hepatobiliary and skeletal disease. Amer. J. Clin. Path. 1963; 40: 349
   PubMed Web of Science ®Google Scholar
• Moss D. W. Properties of alkaline phosphatase isoenzymes separated by starch‐gel electrophoresis. Proc. Ass. Clin. Biochem. 1962; 2: 5
   Google Scholar
• Warnock M. L. Characterization of tissue and serum alkaline phosphatases. Clin. Chim. Acta 1966; 14: 156
   PubMedGoogle Scholar
• Chiandussi L., Greene S. F., Sherlock S. Serum alkaline phosphatase fractions in hepato‐biliary and bone diseases. Clin. Sci. 1962; 22: 425
   PubMed Web of Science ®Google Scholar
• Posen S. M.D. thesis, University of Adelaide. 1966
   Google Scholar
• Metz M., Wilkinson J. H. 1969, unpublished observations
   Google Scholar
• Moss D. W. Iso‐enzymes of alkaline phosphatase in autolysed and butanol‐extracted liver preparations. Nature 1962; 193: 981
   PubMedGoogle Scholar
• Moss D. W., King E. J. Properties of alkaline phosphatase fractions separated by starch‐gel electrophoresis. Biochem. J. 1962; 84: 192
   PubMed Web of Science ®Google Scholar
• Robinson J. C., Pierce J. E. Differential action of neuraminidase on human serum alkaline phosphatase. Nature 1964; 204: 472
   PubMed Web of Science ®Google Scholar
• Butterworth P. J., Moss D. W. Action of neuraminidase on human kidney alkaline phosphatase. Nature 1966; 209: 805
   PubMed Web of Science ®Google Scholar
• Ghosh N. K., Goldman S. S., Fishman W. H. Human placental alkaline phosphatase; a sialoprotein. Enzymologia 1967; 33: 113
   PubMedGoogle Scholar
• Henderson L. W., Metz M., Wilkinson J. H. Serum enzyme elevation in glutethimide intoxication. Brit. Med. J. 1970, (in press)
   Google Scholar
• Schlamowitz M. Production of antibodies against dog intestinal phosphatase. J. Biol. Chem. 1954; 206: 361
   PubMedGoogle Scholar
• Schlamowitz M. The reaction of dog intestinal phosphatase with its antibodies in the region of excess antibody. J. Immun. 1958; 80: 176
   PubMedGoogle Scholar
• Schlamowitz M., Bodansky O. Tissue sources of human serum alkaline phosphatase as determined by immunochemical procedures. J. Biol. Chem. 1959; 234: 1433
   PubMedGoogle Scholar
• Boyer S. H. Human organ alkaline phosphatases: discrimination by several means including starch‐gel electrophoresis of antienzyme‐enzyme supernatant fluids. Ann. N.Y. Acad. Sci. 1963; 103: 938
   PubMed Web of Science ®Google Scholar
• Sussman H. H., Small P. A., Jr., Cotlove E. Human alkaline phosphatase. Immunochemical identification of organ‐specific isoenzymes. J. Biol. Chem. 1968; 243: 160
   PubMed Web of Science ®Google Scholar
• Sussman H. H. Evidence that the increased serum alkaline phosphatase activity in patients with osteomalacia or Paget's disease is from liver phosphatase isoenzymes. Clin. Res. 1968; 16: 130
   Google Scholar
• Sussman H. H. Source of the increased serum alkaline phosphatase activity in Paget's disease. Clin. Chim. Acta 1970; 27: 121
   PubMed Web of Science ®Google Scholar
• Birkett D. J., Done J., Neale F. C., Posen S. Serum alkaline phosphatase in pregnancy: An immunological study. Brit. Med. J. 1966; 1: 1210
   PubMedGoogle Scholar
• Sussman H. H., Bowman M., Lewis J. L. Placental alkaline phosphatases in maternal serum during normal and abnormal pregnancy. Nature 1968; 218: 359
   PubMedGoogle Scholar
• Posen S., Neale F. C., Birkett D. J., Brudenell‐Woods J. Intestinal alkaline phosphatase in human serum. Amer. J. Clin. Path. 1967; 48: 81
   PubMed Web of Science ®Google Scholar
• McMaster Y., Tennant R., Clubb J. S., Neale F. C., Posen S. The mechanism of the elevation of serum alkaline phosphatase in pregnancy. J. Obstet. Gynaec. Brit. Comm. 1964; 71: 735
   PubMedGoogle Scholar
• Latner A. L. Enzymes in Clinical Chemistry, R. Ruyssen, L. Vandendriessche. Elsevier, Amsterdam 1965; 110
   Google Scholar
• Kitchener P. N., Neale F. C., Posen S., Brudenell‐Woods J. Alkaline phosphatase in maternal and fetal sera at term and during the puerperium. Amer. J. Clin. Path. 1965; 44: 654
   PubMed Web of Science ®Google Scholar
• Posen S., Cornish C. J., Horne M., Saini P. K. Placental alkaline phosphatase and pregnancy. Ann. N.Y. Acad. Sci. 1969; 166: 733
   PubMed Web of Science ®Google Scholar
• Seitanidis B., Moss D. W. Serum alkaline phosphatase and 5'‐nucleotidase levels during normal pregnancy. Clin. Chim. Acta 1969; 25: 183
   PubMedGoogle Scholar
• Curzen P., Morris I. Serum heat‐stable alkaline phosphatase in the hypertensive disorders of pregnancy. J. Obstet. Gynaec. Brit. Comm. 1966; 73: 640
   PubMedGoogle Scholar
• Messer R. H. Heat‐stable alkaline phosphatase as an index of placental function. Amer. J. Obstet. Gynec. 1967; 98: 459
   PubMed Web of Science ®Google Scholar
• Shaper A. G., Patel I. Heat‐stable serum alkaline phosphatase of pregnancy in African women. Amer. J. Clin. Path. 1969; 51: 393
   PubMedGoogle Scholar
• McEvoy D., Metz M., Wilkinson J. H. 1969, unpublished observations
   Google Scholar
• Beckman L., Grivea M. Serum alkaline phosphatase variations in pregnant women and new‐born children. Acta Genet. 1965; 15: 218
   PubMedGoogle Scholar
• Robson E. B., Harris H. Genetics of the alkaline phosphatase polymorphism of the human placenta. Nature 1965; 207: 1257
   PubMed Web of Science ®Google Scholar
• Robson E. B., Harris H. Further studies on the genetics of placental alkaline phosphatase. Ann. Hum. Genet. 1966; 30: 219
   Google Scholar
• Keiding N. R. The alkaline phosphatase fractions of human lymph. Clin. Sci. 1964; 26: 291
   PubMed Web of Science ®Google Scholar
• Fishman W. H., Inglis N. I., Krant M. J. Serum alkaline phosphatase of intestinal origin in patients with cancer and with cirrhosis of the liver. Clin. Chim. Acta 1965; 12: 298
   Web of Science ®Google Scholar
• Stolbach L. L., Krant M. J., Inglis N. I., Fishman W. H. Correlation of serum L‐phenylalanine‐sensitive alkaline phosphatase derived from intestine, with the ABO blood group of cirrhotics. Gastroenterology 1967; 52: 819
   PubMedGoogle Scholar
• Beckman L. Associations between human serum alkaline phosphatase and blood groups. Acta Genet. 1964; 14: 286
   PubMedGoogle Scholar
• Stolbach L. L. Clinical application of alkaline phosphatase isoenzyme analysis. Ann. N.Y. Acad. Sci. 1969; 166: 760
   PubMed Web of Science ®Google Scholar
• Bodansky O., Schwartz M. K. 5'‐Nucleotidase. Adv. Clin. Chem. 1968; 11: 277
   PubMedGoogle Scholar
• Hobbs J. R., Campbell D. M., Schuer P. J. Sixth Int. Congr. Clin. Chem., Munich, Vol. 2: Clinical Enzymology. Karger, Basel 1968; 106
   Google Scholar
• Neale F. C., Clubb J. S., Hotchkis D., Posen S. Heat stability of human placental alkaline phosphatase. J. Clin. Path. 1965; 18: 359
   PubMedGoogle Scholar
• Goldbarg J. A., Rutenburg A. M. The colorimetric determination of leucine aminopeptidase in urine and serum of normal subjects and patients with cancer and other diseases. Cancer 1958; 11: 283
   PubMed Web of Science ®Google Scholar
• Cedra J. J., Toskes P. P., Shopa N. A., Wilkinson J. H. The relationship of the serum alkaline phosphatase to urinary hydroxyproline excretion in liver and bone diseases. Clin. Chim. Acta 1970; 27: 437
   PubMedGoogle Scholar
• Fishman W. H., Inglis N. I., Green S., Anstiss C. L., Ghosh N. K., Reif A. E., Rustigian R., Krant M. J., Stolbach L. L. Immunology and biochemistry of Regan isoenzyme of alkaline phosphatase in human cancer. Nature 1968; 219: 697
   PubMed Web of Science ®Google Scholar
• Fishman W. H., Inglis N. I., Stolbach L. L., Krant M. J. A serum alkaline phosphatase isoenzyme of human neoplastic cell origin. Cancer Res. 1968; 28: 150
   PubMed Web of Science ®Google Scholar
• Abelev G. I., Assecritova I. V., Kraevsky N. A., Perova S. D., Perevodchikova N. I. Embryonal serum α‐globulin in cancer patients: diagnostic value. Int. J. Cancer 1967; 2: 551
   PubMed Web of Science ®Google Scholar
• Gold P. Circulating antibodies against carcinoembryonic antigens of the human digestive system. Cancer 1967; 20: 1663
   Web of Science ®Google Scholar
• Bigazzi P. L. La determinazione di nuovi enzimi serici nella diagnosi dell'infarto miocardio, con particolare riguardo alia creatinfosfochinasi. Therapeutikon 1962; 3: 185
   Google Scholar
• King J. Practical Clinical Enzymology. Van Nostrand, Princeton, NJ 1965; 138
   Google Scholar
• Ebashi S., Toyokura Y., Momoi H., Sugita H. High creatine phosphokinase activity of sera of progressive muscular dystrophy. J. Biochem. (Japan) 1959; 46: 103
   Web of Science ®Google Scholar
• Dreyfus J. C., Schapira G., Démos J. Étude de la créatine kinase sérique ches les myopathes et leurs families. Rev. Franç. Etud. Clin. Biol. 1960; 5: 384
   PubMedGoogle Scholar
• Dreyfus J. C., Schapira G., Resnais J., Scebat L. La créatine kinase sérique dans le diagnostic de l'infarctus myocardique. Rev. Franç. Étud. Clin. Biol. 1960; 5: 386
   PubMedGoogle Scholar
• Rosalki S. B. An improved procedure for serum creatine phosphokinase determination. J. Lab. Clin. Med. 1967; 69: 696
   PubMed Web of Science ®Google Scholar
• Ennor A. H., Rosenberg H. Some properties of creatine phosphokinase. Biochem. J. 1954; 57: 203
   PubMed Web of Science ®Google Scholar
• Hughes B. P. A method for the estimation of serum creatine kinase and its use in comparing creatine kinase and aldolase activity in normal and pathological sera. Clin. Chim. Acta 1962; 7: 597
   PubMed Web of Science ®Google Scholar
• Fleisher G. A. Automated method for the determination of serum creatine kinase activity. Clin. Chem. 1967; 13: 233
   PubMed Web of Science ®Google Scholar
• Kuby S. A., Noda L., Lardy H. A. Adenosinetriphosphate‐creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle. J. Biol. Chem. 1954; 209: 191
   PubMed Web of Science ®Google Scholar
• Noda L., Nihei T., Morales M. F. The enzymatic activity and inhibition of adenosine 5'‐triphosphate‐creatine transphosphorylase. J. Biol. Chem. 1960; 235: 2830
   PubMed Web of Science ®Google Scholar
• Tanzer M. L., Gilvarg C. Creatine and creatine kinase measurement. J. Biol. Chem. 1959; 234: 3201
   PubMed Web of Science ®Google Scholar
• Oliver I. T. A spectrophotometric method for the determination of creatine phosphokinase and myokinase. Biochem. J. 1955; 61: 116
   PubMed Web of Science ®Google Scholar
• Rotthauwe H. W., Kowalewski S. Bestimmung der aktivierten Serum‐Kreatin‐Phosphokinase. Z. Klin. Chem. 1967; 5: 254
   PubMedGoogle Scholar
• Hughes B. P. Serum creatine phosphokinase and haemolysis. Clin. Chim. Acta 1968; 21: 287
   PubMedGoogle Scholar
• Wilkinson J. H., Steciw B. Evaluation of a new serum creatine kinase procedure. Clin. Chem. 1970; 16: 370
   PubMedGoogle Scholar
• Thomson W. H. S. An investigation of physical factors influencing the behaviour in vitro of serum creatine phosphokinase and other enzymes. Clin. Chim. Acta 1969; 23: 105
   PubMedGoogle Scholar
• Hess J. W., MacDonald R. P., Natho G. J. W., Murdock K. J. Serum creatine phosphokinase: evaluation of a commercial spectrophotometric method. Clin. Chem. 1967; 13: 994
   PubMed Web of Science ®Google Scholar
• Hess J. W., Murdock K. J., Natho G. J. W. Creatine phosphokinase. A spectrophotometric method with improved sensitivity. Amer. J. Clin. Path. 1968; 50: 89
   PubMed Web of Science ®Google Scholar
• Rosalki S. B. Creatine phosphokinase isoenzymes. Nature 1965; 207: 414
   PubMed Web of Science ®Google Scholar
• Schapira F., Dreyfus J. ‐C., Allard D. Les isoenzymes de la créatine kinase et de l'aldolase du muscle foetal et pathologique. Clin. Chim. Acta 1968; 20: 439
   PubMedGoogle Scholar
• Trainer T. D., Gruenig D. A rapid method for the analysis of creatine phosphokinase isoenzymes. Clin. Chim. Acta 1968; 21: 151
   PubMedGoogle Scholar
• Smith A. F. Diagnostic value of serum‐creatine‐kinase in a coronary‐care unit. Lancet 1967; 2: 178
   PubMed Web of Science ®Google Scholar
• Hunt D., Bailie M. J. The value of serum creatine phosphokinase estimations in the diagnosis of myocardial infarction. Med. J. Aust. 1967; 2: 1031
   PubMedGoogle Scholar
• Ahlborg B., Brohult J. Immediate and delayed metabolic reactions in well‐trained subjects after prolonged physical exercise. Acta Med. Scand. 1967; 182: 41
   PubMed Web of Science ®Google Scholar
• Nygren A. Serum creatine phosphokinase in chronic alcoholism. Acta Med. Scand 1967; 182: 383
   PubMedGoogle Scholar
• Perkoff G. T., Dioso M. M., Bleisch V., Klinkerfuss G. A spectrum of myopathy associated with alcoholism. I. Clinical and laboratory features. Ann. Intern. Med. 1967; 67: 481
   Web of Science ®Google Scholar
• Penneys R., Wilkinson J. H. Elevation of creatine kinase following amputation of the leg. Surgery 1970; 67: 302
   PubMedGoogle Scholar
• Velez‐Garcia E., Hardy P., Dioso M. M., Perkoff G. T. Cysteine‐stimulated serum creatine phosphokinase: unexpected results. J. Lab. Clin. Med. 1966; 68: 636
   PubMedGoogle Scholar
• Graig F. A., Ross G. Serum creatine‐phosphokinase in thyroid disease. Metabolism 1963; 12: 57
   PubMedGoogle Scholar
• Griffiths P. D. Creatinephosphokinase levels in hypothyroidism. Lancet 1963; 1: 894
   PubMedGoogle Scholar
• Perkoff G. T. Demonstration of creatine phosphokinase in human lung tissue. Arch. Intern. Med. 1968; 122: 326
   PubMedGoogle Scholar
• Cohen L. Serum enzyme determinations: Their reliability and value. Med. Clin. N. Amer. 1969; 53: 115
   PubMedGoogle Scholar
• Cherington M., Lewin E., McCrimmon A. Serum creatine phosphokinase changes following needle electromyographic studies. Neurology 1968; 18: 271
   PubMedGoogle Scholar
• Aebi U., Richterich R., Colombo J. P., Rossi E. Progressive muscular dystrophy. II. Biochemical identification of the carrier state in the recessive sex‐linked juvenile (Duchenne) type by serum creatine‐phosphokinase determinations. Enzym. Biol. Clin. 1961–1962; 1: 61
   Google Scholar
• Pearson C. M. Muscular dystrophy: Review and recent observations. Amer. J. Med. 1963; 35: 632
   PubMedGoogle Scholar
• Pearce J. M. S., Pennington R. J. T., Walton J. N. Serum enzyme studies in muscle disease. Part III. Serum creatine kinase activity in relatives of patients with the Duchenne type of muscular dystrophy. J. Neurol. Neurosurg. Psychiat. 1964; 27: 181
   PubMed Web of Science ®Google Scholar
• Milhorat A. T., Shafiq S. A., Goldstone L. Changes in muscle structure in dystrophic patients, carriers and normal siblings seen by electron microscopy; correlation with levels of serum creatine phosphokinase (CPK). Ann. N.Y. Acad. Sci. 1966; 138: 249
   Google Scholar
• Goto I., Peters H. A., Reese H. H. Creatine phosphokinase in neuromuscular disease. Patients and families. Arch. Neurol. 1967; 16: 529
   PubMedGoogle Scholar
• Wieme R. J., Lauryssens M. J. Lactate dehydrogenase multiplicity in normal and diseased human muscle. Lancet 1962; 1: 433
   Google Scholar
• Dawson D. M., Goodfriend T. L., Kaplan N. O. Lactic dehydrogenases: functions of the two types. Science 1964; 143: 929
   PubMed Web of Science ®Google Scholar
• Hudson A. J., Strickland K. P., Wilensky A. J. Serum enzyme studies in familial hyperkalemic periodic paralysis. Clin. Chim. Acta 1967; 17: 331
   PubMedGoogle Scholar
• Barwick D. D. Research in Muscular Dystrophy. Proceedings of the Second Symposium of the Muscular Dystrophy Group, Pitman, London, 1963, 10
   Google Scholar
• Schapira F., Dreyfus J. ‐C., Schapira G., Demos J. Etude de l'aldolase et de la créatine kinase du sérum chez les méres de myopathes. Rev. Franç Étud. Clin. Biol. 1960; 5: 990
   Google Scholar
• Hughes B. P. Serum enzymes in carriers of muscular dystrophy. Brit. Med. J. 1962; 5310: 963
   Google Scholar
• Richterich R., Rosin S., Aebi U., Rossi E. Progressive muscular dystrophy: V. The identification of the carrier state in the Duchenne type by serum creatine kinase determination. Amer. J. Hum. Genet. 1963; 15: 133
   PubMed Web of Science ®Google Scholar
• Wilson K. M., Evans K. A., Carter C. O. Creatine kinase levels in women who carry genes for three types of muscular dystrophy. Brit. Med. J. 1965; 5437: 750
   Google Scholar
• Emery A. E. H. Carrier detection in sex‐linked muscular dystrophy. J. Hum. Genet. 1965; 14: 318
   Google Scholar
• Thompson M. W., Murphy E. G., McAlpine P. J. An assessment of the creatine kinase test in the detection of carriers of Duchenne muscular dystrophy. J. Pediat. 1967; 71: 82
   PubMed Web of Science ®Google Scholar
• Lyon M. F. Gene action in the X‐chromosome of the mouse. Nature 1961; 190: 372
   PubMed Web of Science ®Google Scholar
• Emery A. E. H. Lyonisation of the X‐chromosome. Lancet 1964; 1: 884
   Google Scholar
• Pearson C. M., Fowler W. M., Jr., Wright S. W. X‐chromosome mosaicism in females with muscular dystrophy. Proc. Nat. Acad. Sci. 1963; 50: 24
   PubMedGoogle Scholar
• Dawson D. M., Eppenberger H. M., Kaplan N. O. The comparative enzymology of creatine kinases. II. Physical and chemical properties. J. Biol. Chem. 1967; 242: 210
   PubMed Web of Science ®Google Scholar
• Schapira F., Dreyfus J. ‐C., Allard D. Les isozymes de la créatine kinase et de l'aldolase du muscle foetal et pathologique. Clin. Chim. Acta 1968; 20: 439
   PubMedGoogle Scholar
• Kar N. C., Pearson C. M. Creatine phosphokinase isoenzymes in muscle in human myopathies. Amer. J. Clin. Path. 1965; 43: 207
   PubMed Web of Science ®Google Scholar
• Miyazaki K., Toyoda R., Tomino H., Yoshimatsu M., Saijo K., Katsunuma N., Fujino A. Saishin Igaku 1965; 20: 202, (Quoted by Schapira et al.205)
   PubMedGoogle Scholar
• Milhorat A. T., Goldstone L. The carrier state in muscular dystrophy of the Duchenne type. Identification by serum creatine kinase level. J.A.M.A. 1965; 194: 130
   PubMed Web of Science ®Google Scholar
• Rotthauwe H. W., Kowalewski S. Klinische und biochemische Untersuchungen bei Myopathien: II. Die Bedeutung der Serum‐Kreatin Phosphokinase und der Serum‐Aldolase für die Identifizierung von Heterozygoten der recessiv x‐chromosomalen Formen der progressiven Muskel‐dystrophie (Typ III a und b). Klin. Wschr. 1965; 43: 150
   Google Scholar
• Herschkowitz N., Cumings J. N. Creatine kinase in cerebrospinal fluid. J. Neurol. Neurosurg. Psychiat. 1964; 27: 247
   PubMed Web of Science ®Google Scholar
• Acheson J., James D. C., Hutchinson E. C., Westhead R. Serum‐creatine‐kinase levels in cerebral vascular disease. Lancet 1965; 1: 1306
   Web of Science ®Google Scholar
• Langton L., Moxon C. P., Riddoch D., Westhead R. A., Woolf A. L. Jugular bulb creatine kinase as an indication of slight transient brain damage. Lancet 1967; 2: 278
   PubMedGoogle Scholar
• Belton N. R., Backus R. E., Millichap J. G. Serum creatine phosphokinase activity in epilepsy. Clinical and experimental studies. Neurology 1967; 17: 1073
   PubMedGoogle Scholar
• Meltzer H. Creatine kinase and aldolase in serum: Abnormality common to acute psychoses. Science 1968; 159: 1368
   PubMed Web of Science ®Google Scholar
• Smith J. B., Healy P. J. Elevated serum creatine phosphokinase activity in diseases of the central nervous system in sheep. Clin. Chim. Acta 1968; 21: 295
   PubMed Web of Science ®Google Scholar
• Saito M., Hibi I., Kawajura M., Fukuyama Y. Creatinephosphokinase levels in hypothyroidism. Lancet 1963; 2: 252
   Google Scholar
• Graig F. A., Smith J. C. Serum creatine phosphokinase activity in altered thyroid states. J. Clin. Endocr. 1965; 25: 723
   PubMed Web of Science ®Google Scholar
• Griffiths P. D. Serum enzymes in diseases of the thyroid gland. J. Clin. Path. 1965; 18: 660
   PubMed Web of Science ®Google Scholar
• Fleisher G. A., McConahey W. M., Pankow M. Serum creatine kinase, lactic dehydrogenase, and glutamic oxalacetic transaminase in thyroid diseases and pregnancy. Mayo Clin. Proc. 1965; 40: 300
   PubMed Web of Science ®Google Scholar
• Itelson J., Rubinstein J., Gaist L., Ménaché R. La place des variations de l'activité de la créatine kinase, sérique parmi les tests de la fonction thyroidienne. Rev. Franç. Étud. Clin. Biol. 1968; 13: 905
   PubMedGoogle Scholar
• Askonas B. A. Effect of thyroxine on creatinephosphokinase activity. Nature 1951; 167: 933
   PubMed Web of Science ®Google Scholar
• Den Bakker P. B., Sundermeyer J. F., Wendt V. E., Salhaney M., Gudbjarnason S., Bing R. J. Myocardial metabolism in a patient with Hashimoto's thyroiditis and hypothyroidism. Amer. J. Med. 1962; 32: 822
   PubMedGoogle Scholar
• Lanza A. Creatine kinase in serum after uterus contraction produced by oxytocin. Experientia 1968; 24: 337
   PubMedGoogle Scholar
• Griffiths P. D. Serum levels of ATP: creatine phosphotransferase (creatine kinase). The normal range and effect of muscular activity. Clin. Chim. Acta 1966; 13: 413
   PubMedGoogle Scholar
• Griffiths P. D. The activity of ATP: creatine phosphotransferase (E.C.2.7.3.2) in umbilical cord blood. Clin. Chim. Acta 1968; 20: 465
   PubMedGoogle Scholar
• Rudolph N., Gross R. T. Creatine phosphokinase activity in serum of newborn infants as an indicator of fetal trauma during birth. Pediatrics 1966; 38: 1039
   PubMedGoogle Scholar
• Maclean D., Griffiths P. D., Emslie‐Smith D. Serum‐enzymes in relation to electrocardiographic changes in accidental hypothermia. Lancet 1968; 2: 1266
   PubMedGoogle Scholar
• Schmidt E., Schmidt F. W., Möhr J. An improved simple chromatographic method for separating the isoenzymes of malic dehydrogenase and glutamic oxaloacetic transaminase. Clin. Chim. Acta 1967; 15: 337
   Google Scholar
• Boyde T. R. C. Detection and assay of mitochondrial aspartate aminotransferase in serum. Z. Klin. Chem. 1968; 6: 431
   PubMedGoogle Scholar
• Schmidt E., Schmidt F. W., Otto P. Isoenzymes of malic dehydrogenase, glutamic oxaloacetic transaminase and lactic dehydrogenase in serum in diseases of the liver. Clin. Chim. Acta 1967; 15: 283
   Google Scholar
• Gabrieli E. R., Orfanos A. A clinical study of serum glutamic oxalacetic transaminase isoenzymes in liver diseases. Proc. Soc. Exp. Biol. Med. 1968; 128: 803
   PubMedGoogle Scholar
• Boyde T. R. C. Serum levels of the mitochondrial isoenzyme of aspartate aminotransferase in myocardial infarction and muscular dystrophy. Enzym. Biol. Clin. 1968; 9: 385
   PubMedGoogle Scholar
• Massarat S., Lang N. Immunologie und Enzymkinetik der Glutamat‐Oxalacetat‐Transaminase (GOT) und der Glutamat‐Pyrovat‐Transaminase (GPT). III. Mitteilung. Untersuchungen zur Immunhemmung der Transaminasen im Serum von Leberkranken und von Patienten mit Herzinfarkt. Klin. Wschr. 1965; 43: 602
   PubMedGoogle Scholar
• Mannucci P. M., Ideo G., Cao A., Macciotta A. Gli isoenzimi della latticodeidrogenasi (LDH) e della transaminasi glutammico‐ossalacetica (TGO) nel muscolo fetale, adulto, e di soggetti affetti da distrofia muscolare progressiva tipo Duchenne. Rass. Med. Sarda 1965; 68: 287
   PubMedGoogle Scholar
• Schwartz M. K., Bodansky O. Relationship of the electrophoretic patterns of phosphohexose isomerase and glutamic oxaloacetic transaminase in human tissues to the patterns in serum of patients with neoplastic disease. Amer. J. Med. 1966; 40: 231
   PubMedGoogle Scholar
• Gabrieli E. R., Orfanos A. Effect of carbon tetrachloride on serum glutamic‐oxalacetic transaminase isoenzymes. Proc. Soc. Exp. Biol. Med. 1968; 127: 766
   PubMedGoogle Scholar
• Fleisher G. A., Potter C. S., Wakim K. G. Separation of 2 glutamic‐oxalacetic transaminases by paper electrophoresis. Proc. Soc. Exp. Biol. Med. 1960; 103: 229
   PubMed Web of Science ®Google Scholar
• Boyd J. W. The intracellular distribution latency and electrophoretic mobility of L‐glutamate‐oxaloacetate transaminase in rat liver. Biochem. J. 1961; 81: 434
   PubMed Web of Science ®Google Scholar
• Boyd J. W. The extraction and purification of two isoenzymes of L‐aspartate: 2‐oxoglutarate amino‐transferase. Biochim. Biophys. Acta 1966; 113: 302
   PubMedGoogle Scholar
• Bodansky O., Schwartz M. K., Nisselbaum J. S. Isozymes of aspartate aminotransferase in tissues and blood of man. Adv. Enzyme Regulat. 1966; 4: 299
   PubMedGoogle Scholar
• Martinez‐Carrion M., Turano C., Chiancone E., Bossa F., Giastosio A., Riva F., Fasella P. Isolation and characterization of multiple forms of glutamate aspartate aminotransferase from pig heart. J. Biol. Chem. 1967; 242: 2397
   PubMed Web of Science ®Google Scholar
• Martinez‐Carrion M., Tiemeier D. Mitochondrial glutamate‐aspartate transaminase. I. Structural comparison with supernatant isozyme. Biochemistry 1967; 6: 1715
   PubMed Web of Science ®Google Scholar
• Decker L. E., Rau E. M. Multiple forms of glutamic‐oxalacetic transaminase in tissues. Proc. Soc. Exp. Biol. Med. 1963; 112: 144
   PubMed Web of Science ®Google Scholar
• Michuda C. M., Martinez‐Carrion M. Mitochondrial aspartate transaminase. II. Isolation and characterization of the multiple forms. Biochemistry 1969; 8: 1095
   PubMedGoogle Scholar
• Boyde T. R. C. The interaction between α2‐macroglobulin and cationic aspartate aminotransferase. Biochem. J. 1969; 111: 59
   PubMedGoogle Scholar