1
Views
6
CrossRef citations to date
0
Altmetric
Original Article

Activity of α-Amylase and α-1,4-Glucosidase in Subfractions of Human Liver Homogenates

&
Pages 209-213 | Received 27 Mar 1972, Accepted 16 Jun 1972, Published online: 08 Jul 2009

References

  • Auricchio F., Bruni C. B., Sica V. Further purification and characterization of the acid α-glucosidase. Biochem. J. 1968; 108: 161
  • Belenky D. M., Rosenfeld E. L. The splitting of glycogen and maltose by rabbit γ-amylase in the presence of various sugars and their derivatives. Biochimija (Russ) 1967; 32: 1201
  • Björntorp P., Björkerud S., Scherstén T. Subcellular fractionation of human liver. Biochim. biophys. Acta (Amst.) 1965; 111: 375
  • Brown B. I., Brown D. H. The subcellular distribution of enzymes in type II glycogenosis and the occurrence of an oligo-α-1,4-glucan glycohydrolase in human tissues. Biochim. biophys. Acta (Amst.) 1965; 110: 124
  • Ceska M., Birath K., Brown B. A new rapid method for the clinical determination of α-amylase activities in human serum and urine. Optimal conditions. Clin. chim. Acta 1969; 26: 437
  • Cohn Z. A., Fedorko, Martha. The formation and fate of lysosomes. Lysosomes in Biology and Pathology, J. T. Dingle, H. B. Fell. North-Holland Publ. Comp., Amsterdam, London 1969; Vol. 1: 43
  • Daems W. Th., Wisse E., Brederoo P. Electron microscopy of the vacuolar apparatus. Lysosomes in Biology and Pathology, J. T. Dingle, H. B. Fell. North-Holland Publ. Comp., Amsterdam, London 1969; Vol. 1: 64
  • deDuve C. The lysosome in retrospect. Lysosomes in Biology and Pathology, J. T. Dingle, H. B. Fell. North-Holland Publ. Comp., Amsterdam, London 1969; Vol. 1: 3
  • deDuve C., Baudhuin P. Peroxisomes (microbodies and related particles). Physiol. Rev. 1966; 46: 323
  • deDuve C., Pressman B. C., Gianetto R., Wattiaux R., Appelmans S. Tissue fractionation studies; intracellular distribution patterns of enzymes in rat-liver tissue. Biochem. J. 1955; 60: 604
  • Gamklou R., Scherstén T. Activity of α-Amylase and α-1,4-Glucosidase in human liver tissue. Scand. J. clin. Lab. Invest. 1972; 30: 00
  • Gianetto R., deDuve C. Tissue fractionation studies. 4. Comparative study of the binding of acid phosphatase, β-glucuronidase and cathepsin by rat liver particles. Biochem. J. 1955; 59: 433
  • Lejeune N., Thinès-Sempoux D., Hers H. G. Tissue fractionation studies. 6. Intracellular distribution and properties of α-glucosidases in rat liver. Biochem. J. 1963; 86: 16
  • Lowry O. H., Rosenbrough N. J., Farr A. L., Randall R. J. Protein measurement with Folin phenol reagent. J. biol. Chem. 1951; 193: 265
  • Lucy J. A. Lysosomal membranes. Lysosomes in Biology and Pathology, J. T. Dingle, H. B. Fell. North-Holland Publ. Comp., Amsterdam, London 1969; Vol. 2: 313
  • Potter V. R., Umbreit W. W., Burris R. N., Stauffer J. F. Manometric Techniques. Mineapolis, Burgess 1959; 170
  • Schneider W. C. Phosphorus compounds in animal tissues; extraction and estimation of desoxypentose nucleic acid and of pentose nucleic acid. J. biol. Chem. 1945; 161: 293
  • Tappel A. L., Sawant P. L., Shibko S. Lysosomes: distribution in animals, hydrolytic capacity and other properties. Lysosomes, A. V. S. de Reuckl, M. P. Cameron. J. & A. Churchilll, London 1963; 78
  • Torres H. N., Olavarria J. M. Metabolism of malto-oligosaccharides. Acta physiol. lat.-amer. 1961; 11: 95
  • Torres H. N., Olavarria J. M. Liver α-glucosidases. J. biol. Chem. 1964; 239: 2427

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.