Muscle Protein Analysis by Two-Dimensional Gel Electrophoresis

References

• Dawson D. M., Eppenbenger H. M., Eppenberger M. E. Multiple molecular forms of creatine kinases. Ann. N.Y. Acad. Sci. 1968; 151: 616
   PubMed Web of Science ®Google Scholar
• Martonosi A., Halpin R. A. Sarcoplasmic reticulum. X. The protein composition of sarcoplasmic reticulum membranes. Arch. Biochem. Biophys. 1971; 144: 66
   PubMed Web of Science ®Google Scholar
• Berg D. K., Kelly R. B., Sargent P. B., Williamson P., Hall Z. W. Binding of a-bungarotoxin to acetylcholine receptors in mammalian muscle. Proc. Natl. Acad. Sci. U.S.A. 1972; 69: 147
   PubMed Web of Science ®Google Scholar
• Sender P. M. Muscle myofibrils: solubilization and gel electrophoresis. FEBS Leit. 1971; 17: 106
   PubMed Web of Science ®Google Scholar
• Pette D., Vrbova G., Whalen R. C. Independent development of contractile properties and myosin light chains in embryonic chick fast and slow muscle. Pfluegers Arch. 1979; 378: 251
   PubMed Web of Science ®Google Scholar
• Otarrell P. H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 1975; 250: 4007
   PubMed Web of Science ®Google Scholar
• Barrett E. J., Headon Denis R. Two-dimensional polyacrylamide gel electrophoresis of rabbit skeletal muscle microsomal proteins. FEBS Lett. 1975; 51: 121
   PubMed Web of Science ®Google Scholar
• Stegemann H. Proteinfraktionierungen in Polyacrylamid und die Anwendung auf die Genetische Analyse bei Pflanzen. Agnew. Chem. 1970; 82: 640
   Google Scholar
• Weber K., Osborn M. The reliability of molecular weight determinations of dodecyl sulfate- polyacrylamide gel electrophoresis. J. Biol. Chem. 1969; 244: 4406
   PubMed Web of Science ®Google Scholar
• Siemankowski R. F., Dreizen R. Canine cardiac myosin with special reference to pressure overload cardiac hypertrophy. J. Biol. Chem. 1978; 253: 8648
   PubMed Web of Science ®Google Scholar
• Tuszynski G. P., Buck C. A., Warren L. A two-dimensional polyacrylamide gel electrophoresis (PAGE) system using sodium dodecyl suIfate-PAGE in the first dime'nsion. Anal. Biochem. 1979; 93: 329
   PubMed Web of Science ®Google Scholar
• Otarrell P. Z., Goodman H. M., Otarrell P. H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 1977; 12: 1133
   PubMed Web of Science ®Google Scholar
• Willard K. E., Giometti C. S., Anderson N. L., O'Connor T. E., Anderson N. G. Analytical techniques for cell fractions. XXVI. A two-dimensional electrophoretic analysis of basic proteins using phosphatidyl choline/urea solubilization. Anal. Biochem. 1979; 100: 289
   PubMed Web of Science ®Google Scholar
• Giometti C. S., Anderson N. G., Anderson N. L. Muscle protein analysis. J. High-resolution two-dimensional electrophoresis of skeletal muscle proteins for analysis of small biopsy samples. Clin. Chem. 1979; 25: 1877
   PubMed Web of Science ®Google Scholar
• Man N. T., Morris G. E., Cole R. J. Two-dimensional gel analysis of nuclear proteins during muscle differentiationin vitro.1. Changes in nuclear protein content. Exp. Cell Res. 1980; 126: 375
   PubMed Web of Science ®Google Scholar
• MacGillivray A. J., Johnston C, MacFarlane R., Rickwood D. The isolation and partial characterization of low-molecular-weight phosphorylated component of the non-histone proteins of mouse nuclei. Biochem. J. 1978; 175: 35
   PubMed Web of Science ®Google Scholar
• Klose J., Wallenberg-Pachaly H. Changes of soluble protein populations during organogenesis of mouse embryos as revealed by protein mapping. Rev. Biol. 1976; 51: 324
   Google Scholar
• Garrels J. I. Two-dimensional gel electrophoresis and computer analysis of proteins synthesized by clonal cell lines. J. Biol. Chem. 1979; 254: 7961
   PubMed Web of Science ®Google Scholar
• Anderson N. G., Anderson N. L. Molecular anatomy. Behring Inst. Mill. 1979; 63: 169
   Google Scholar
• McConkey E. H., Taylor B. J., Phan D. Human heterozygosity: a new estimate. Proc. Natl. Acad. Sci. U.S.A. 1979; 76: 6500
   PubMed Web of Science ®Google Scholar
• Walton K. E., Styer D., Gruenstein E. I. Genetic polymorphism in normal human fibroblasts as analyzed by two-dimensional polyacrylamide gel electrophoresis. J. Biol. Chem. 1979; 254: 7951
   PubMed Web of Science ®Google Scholar
• Anderson N. G., Anderson N. L. Analytical techniques for cell fractions. XXI. Two-dimensional analysis of serum and tissue proteins: multiple isoelectric focusing. Anal. Biochem. 1978; 85: 331
   PubMed Web of Science ®Google Scholar
• Anderson N. L., Anderson N. G. Analytical techniques for cell fractions. XXII. Two-dimensional analysis of serum and tissue proteins: multiple gradient slab-gel electrophoresis. Anal. Biochem. 1978; 85: 341
   PubMed Web of Science ®Google Scholar
• Tanford C., Reynolds J. A. Characterization of membrane proteins in detergent solutions. Biochim. Biophys. Acta 1976; 457: 133
   PubMed Web of Science ®Google Scholar
• Vandenburgh H., Kaufman S. Protein degradation in embryonic skeletal muscle. J. Biol. Chem. 1980; 255: 5826
   PubMed Web of Science ®Google Scholar
• Ribolow H., Barany K., Steinschneider A., Barany M. Lack of phosphate incorporation into TN-1 in live frog muscle. Arch. Biochem. Biophys. 1977; 179: 81
   PubMed Web of Science ®Google Scholar
• Anderson N. L., Hickman B. J. Analytical techniques for cell fractions. XXIV. Isoelectric point standards for two-dimensional electrophoresis. Anal. Biochem. 1979; 93: 321
   PubMed Web of Science ®Google Scholar
• Bonner W. M., Laskey R. A. A film detection method for tritium-labeled proteins and nucleic acids in polyacrylamide gels. Eur. J. Biochem. 1974; 46: 83
   PubMedGoogle Scholar
• Whalen R. G., Butler-Browne G. S., Gros F. Identification of a novel form of myosin light chain present in embryonic muscle tissue and cultured muscle cells. J. Mol. Biol. 1978; 126: 415
   PubMed Web of Science ®Google Scholar
• Yablonka Z., Yaffe D. Synthesis of myosin light chains and accumulation of translatable mRNA coding for light chain-like polypeptides in differentiating muscle cultures. Differentiation 1977; 8: 133
   PubMed Web of Science ®Google Scholar
• Garrels J. I. Changes in protein synthesis during myogenesis in a clonal cell line. Dev. Biol. 1979; 73: 134
   PubMed Web of Science ®Google Scholar
• Giometti C. S., Anderson N. G. Muscle protein analysis. III. Analysis of solubilized frozen-tissue sections by two-dimensional electrophoresis. Clin. Chem. 1981; 27: 1918
   PubMed Web of Science ®Google Scholar
• Switzer R. C, III, Merril C. R., Shifrin S. A highly sensitive silver stain for detecting proteins and peptides in polyacrylamide gels. Anal. Biochem. 1979; 98: 231
   PubMed Web of Science ®Google Scholar
• Merril C. R., Switzer R. C., Van Keuren M. L. Trace polypeptides in cellular extracts and human body fluids detected by two-dimensional electrophoresis and highly sensitive silver stain. Proc. Nail. Acad. Sci. U.S.A. 1979; 76: 4335
   PubMed Web of Science ®Google Scholar
• Oakley B. R., Kirsch D. R., Morris N. R. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 1980; 105: 361
   PubMed Web of Science ®Google Scholar
• Sammons D. W., Adams L. D., Nishizawa E. E. Ultrasensitive silver-based color staining of polypeptides in polyacrylamide gels. Electrophoresis 1981; 2: 135
   Web of Science ®Google Scholar
• Furukawa T., Peter J. B. The muscular dystrophies and related disorders. I. The muscular dystrophies. JAMA 1978; 239: 1537
   PubMed Web of Science ®Google Scholar
• Furukawa T., Peter J. B. The muscular dystrophies and related disorders. II. Diseases simulating muscular dystrophies. JAMA 1978; 239: 1654
   PubMed Web of Science ®Google Scholar
• Devlin R. B., Emerson C. P., Jr. Coordinate regulation of contractile protein synthesis during myoblast differentiation. Cell 1978; 13: 599
   PubMed Web of Science ®Google Scholar
• Carmon Y., Neuman S., Yaffe D. Synthesis of tropomyosin in myogenic cultures and in RNA-direcied cell-free systems: qualitative changes in the polypeptides. Cell 1978; 14: 393
   PubMed Web of Science ®Google Scholar
• Patterson B., Strohman R. C. Myosin synthesis in cultures of differentiating chicken embryo skeletal muscle. Dev. Biol. 1972; 29: 113
   PubMed Web of Science ®Google Scholar
• Emerson C. P., Beckner S. K. Activation of myosin synthesis in fusing and mononucleated myoblasts. J. Mol. Biol. 1975; 93: 431
   PubMed Web of Science ®Google Scholar
• Fambrough D., Rash J. E. Development of acetylcholine sensitivity during myogenesis. Dev. Biol. 1971; 26: 55
   PubMed Web of Science ®Google Scholar
• Merlie J. P., Sobel A., Changeux J. P., Gros F. Synthesis of acetylcholine receptor during differentiation of cultured embryonic muscle cells. Proc. Nail. Acad. Sci. U.S.A. 1975; 72: 4028
   PubMed Web of Science ®Google Scholar
• Prives J. M., Paterson B. M. Differentiation of cell membranes in cultures of embryonic chick breast muscle. Proc. Natl. Acad. Sci. U.S.A. 1974; 71: 3208
   PubMed Web of Science ®Google Scholar
• Wilson B. W., Nieberg P. S., Walker C. R., Linkhart T. A., Fry D. M. Production and release of acetylcholinesterase by cultured chick embryo muscle. Dev. Biol. 1973; 33: 285
   PubMed Web of Science ®Google Scholar
• Turner D. C, Maier V., Eppenberger H. M. Creatine kinase and aldolase isoenzyme transitions in cultures of chick skeletal muscle cells. Dev. Biol. 1974; 37: 63
   PubMed Web of Science ®Google Scholar
• Yaffe D., Fuchs S. Autoradiographic study of the incorporation of uridine-'H during myogenesis in tissue culture. Dev. Biol. 1967; 15: 33
   PubMed Web of Science ®Google Scholar
• Konigsberg I. R. Diffusion-mediated control of myoblast fusion. Dev. Biol. 1971; 26: 133
   PubMed Web of Science ®Google Scholar
• Keller L. R., Emerson C. P., Jr. Synthesis of adult myosin light chains by embryonic muscle cultures. Proc. Natl. Acad. Sci. U.S.A. 1980; 77: 1020
   PubMed Web of Science ®Google Scholar
• Yaffe D. Retention of differentiation potentialities during prolonged cultivation of myogenic cells. Proc. Natl. Acad. Sci. U.S.A. 1968; 61: 477
   PubMed Web of Science ®Google Scholar
• Garrels J. I., Gibson W. Identification and characterization of multiple forms of actin. Cell 1976; 9: 793
   PubMed Web of Science ®Google Scholar
• Whalen R. G., Butler-Browne G. S., Gros F. Protein synthesis and actin heterogeneity in calf muscle cells in culture. Proc. Natl. Acad. Sci. U.S.A. 1976; 73: 2018
   PubMed Web of Science ®Google Scholar
• Storti R. V., Horovitch S. J., Scott M. P., Rich A., Pardue M. L. Myogenesis in primary cell cultures from Drosophila melanogaster: protein synthesis and actin heterogeneity during development. Cell 1978; 13: 589
   PubMed Web of Science ®Google Scholar
• Whalen R. G., Buckingham M. E., Goto S., Merlie J. P., Gros F. The patterns and control of protein synthesis in cultured calf muscle cells. Pathogenesis of Human Muscular Dystrophies. Excerpta Medica, Amsterdam 1977; 433
   Google Scholar
• Gruenstein E., Rich A. Non-identity of muscle and non-muscle actins. Biochem. Biophys. Res. Commun. 1975; 64: 472
   PubMed Web of Science ®Google Scholar
• Fyrberg E. A., Donady J. J. Actin heterogeneity in primary embryonic culture cells from. Drosophila melanogaster, Dev. Biol. 1979; 68: 487
   PubMed Web of Science ®Google Scholar
• Zechel K. Localization of the charge differences in the actins of rabbit skeletal muscle and chicken gizzard by two-dimensional gel electrophoretic analysis of tryptic fragments. Hoppe-Seyler's Z. Physiol. Chem… 1979; 360: 777
   PubMedGoogle Scholar
• Hunter T., Garrels J. I. Characterization of the mRNAs fora-, /S-, and y-actin. Cell 1977; 12: 767
   PubMed Web of Science ®Google Scholar
• Mak A. S., Smillie L. B., Stewart G. R. A comparison of the amino acid sequences of rabbit skeletal muscle α- and β-tropomyosins. J. Biol. Chem. 1980; 255: 3647
   PubMed Web of Science ®Google Scholar
• Cohen I., Cohen C. A tropomyosin-like protein from human platelets. J. Mol. Biol. 1972; 68: 383
   PubMed Web of Science ®Google Scholar
• Fine R. E., Blitz A. L., Hitchcock S. E., Kaminer B. Tropomyosin in brain and growing neurones. Nature (London), New Biol 1973; 245: 182
   PubMedGoogle Scholar
• Bárány M., Close R. J. The transformation of myosin in cross-reinnervated rat muscle. J. Physiol. 1971; 213: 455
   PubMedGoogle Scholar
• Salmons S., Sreter F. A. Significance of impulse activity in the transformation of skeletal muscle type. Nature (London) 1976; 263: 30
   PubMed Web of Science ®Google Scholar
• Stockdale F. E., Raman N., Baden H. Myosin light chains and the developmental origin of fast muscle. Proc. Natl. Acad. Sci. U.S.A. 1981; 78: 931
   PubMed Web of Science ®Google Scholar
• Gauthier G. F., Lowey S., Hobbs A. W. Fast and slow myosin in developing muscle fibers. Nature (London). 1978; 274: 25
   PubMed Web of Science ®Google Scholar
• Merlie J. P., Changeux J., Gros F. Skeletal muscle acetylcholine receptor. J. Biol. Chem. 1978; 253: 2882
   PubMed Web of Science ®Google Scholar
• Blau H. M., Epstein C. J. Manipulation of myogenesisin vitro:Reversible inhibition by DM SO. Cell 1979; 17: 95
   PubMed Web of Science ®Google Scholar
• Ha D. B., Boland R., Martonosi A. Synthesis of the calcium transport ATPase of sarcoplasmic reticulum and other muscle proteins during development of muscle cellsin vivoand in vitro, Biochim. Biophys. Acta 1979; 585: 165
   PubMedGoogle Scholar
• Brzeski H., Linder S., Krondahl U., Ringertz N. R. Pattern of polypeptide synthesis in myoblast hybrids. Exp. Cell Res. 1980; 128: 267
   PubMed Web of Science ®Google Scholar
• Britch M., Allen T. D. The effects of cytochalasin B on the cytoplasmic contractile network revealed by whole-cell transmission electron microscopy. Exp. Cell. Res. 1981; 131: 161
   PubMed Web of Science ®Google Scholar
• Devlin R. B., Emerson C. P., Jr. Coordinate accumulation of contractile protein mRNAs during myoblast differentiation. Dev. Biol. 1979; 69: 202
   PubMed Web of Science ®Google Scholar
• Breton R., Fiszman M., Gros F. Chick embryo cardiocytes in culture synthesize proteins not present in embryonic heart. Biochem. Biophys. Res. Commun. 1980; 95: 281
   PubMed Web of Science ®Google Scholar
• Lee C, Charles D., Bronson D., Griffin M., Bennett L. Analyses of mouse andDrosophilaproteins by two-dimensional gel electrophoresis. Mol. Gen. Genet. 1979; 176: 303
   PubMedGoogle Scholar
• Dawson D. M., Eppenberger H. M., Kaplan N. O. The comparative enzymology of creatine kinase. 11. Physical and chemical properties. J. Biol. Chem. 1967; 242: 210
   PubMed Web of Science ®Google Scholar
• Henslee J. G, Srere P. A. Resolution of rat mitochondrial matrix proteins by two-dimensional polyacrylamide gel electrophoresis. J. Biol. Chem. 1979; 254: 5488
   PubMed Web of Science ®Google Scholar
• Liew C., Sole M. J. Nuclear proteins in the heart of the cardiomyopathic Syrian hamster. Fractionation of phenol soluble nonhistone proteins by two-dimensional polyacrylamide gel electrophoresis. Ore. Res. 1978; 42: 628
   Google Scholar
• Izant J. G., Lazarides E. lnvariance and heterogeneity in the major structural and regulatory proteins of chick muscle cells revealed by two-dimensional gel electrophoresis. Proe. Nail. Acad. Sci. U.S.A. 1977; 74: 1450
   PubMed Web of Science ®Google Scholar
• Lazarides E., Balzer D. R. Jr., Specificity of desmin to avian and mammalian muscle cells. Cell. 1978; 14: 429
   PubMed Web of Science ®Google Scholar
• Granger B. L., Lazarides E. Desmin and vimentin coexist at the periphery of the myofibril Z disc. Cell 1979; 18: 1053
   PubMed Web of Science ®Google Scholar
• Gard D. L., Bell P. B., Lazarides E. Coexistence of desmin and the fibroblastic intermediate filament subunit in muscle and nonmuscle cells: Identification and comparative peptide analysis. Proc. Natl. Acad. Sci. U.S.A. 1979; 76: 3894
   PubMed Web of Science ®Google Scholar
• O'Connor C. M., Balzer D. R., Lazarides E. Phosphorylation of subunit proteins of intermediate filaments from chicken muscle and nonmuscle cells. Proc. Natl. Acad. Sci. U.S.A. 1979; 76: 819
   PubMed Web of Science ®Google Scholar
• Wang C, Asai D. J., Lazarides E. The 68,000-dalton neurofilament-associated polypeptide is a component of nonneuronal cells and of skeletal myofibrils. Proc. Natl. Acad. Sci. U.S.A. 1980; 77: 1541
   PubMed Web of Science ®Google Scholar
• Fellini S. A., Bennett G. S., Toyama Y., Holtzer H. Biochemical and immunological heterogeneity of 100 A filament subunits from different chick cell types. Differentiation 1978; 12: 59
   PubMed Web of Science ®Google Scholar
• Giometti C. S., Barany M., Danon M. J., Anderson N. G. Muscle protein analysis. 11. Two-dimensional electrophoresis of normal and diseased human skeletal muscle. Clin. Chem. 1980; 26: 1152
   PubMed Web of Science ®Google Scholar
• Fardeau M., Godet-Guillain J., Tome F. M. S., Carson S., Whalen R. G. Congenital neuromuscular disorders: a critical review. Current Topics in Nerve and Muscle Research, G.A. J. Karpati. Excerpta Medica, Aguayo, Amsterdam 1977; 164
   Google Scholar
• Johnson M. A., Polgar J., Weightman D., Appleton D. Data on the distribution of fiber types in thirty-six human muscles: an autopsy study. J. Neurol. Sci. 1973; 18: 111
   PubMed Web of Science ®Google Scholar
• Mak A., Smillie L. B., Barany M. Specific phosphorylation at serine-283 of a-tropomyosin from frog skeletal and rabbit skeletal and cardiac muscle. Proc. Natl. Acad. Sci. U.S.A. 1978; 75: 3588
   PubMed Web of Science ®Google Scholar
• Perry S. V., Cole H. A. Phosphorylation of troponin and the effects of interactions between the components of the complex. Biochem. J. 1974; 141: 733
   PubMed Web of Science ®Google Scholar
• Perrie W. T., Smillie L. B., Perry S. V. A phosphorylated light chain component of myosin from skeletal muscle. Cold Spring Harbor Symp. Quant. Biol. 1972; 37: 17
   Google Scholar
• Janis R. A., Moat-Staats B. M., Gualtier R. T. Protein phosphorylation during spontaneous contraction of smooth muscle. Biochem. Biophys. Res. Commun. 1980; 96: 265
   PubMed Web of Science ®Google Scholar
• Barron J. T., Barany M., Barany K., Storti R. V. Reversible phosphorylation and dephosphorylation of the 20,000-dalton light chain of myosin during the contraction-relaxation-contraction cycle of arterial smooth muscle. J. Biol. Chem. 1980; 255: 6238
   PubMed Web of Science ®Google Scholar
• Janis R. A., Barany K., Barany M., Sarmiento J. G. Association between myosin light chain phosphorylation and contraction of uterine smooth muscle. Mol. Physiol. 1981; 1: 3
   Google Scholar
• Steinbach J. H., Schubert D., Eldridge L. Changes in cat muscle contractile proteins after prolonged muscle inactivity. Exp. Neurol. 1980; 67: 655
   PubMed Web of Science ®Google Scholar
• Danon M. J., Giometti C. S., Manaligod J. R., Perurena O. H., Skosey J. L. Adult onset nemaline rods in a patient treated for suspected dermatomyositis: a study with two-dimensional electrophoresis. Arch. Neurol. 1981; 38: 761
   PubMedGoogle Scholar
• Libera L., Sartore S., Schiafflno S. Comparative analysis of chicken atrial and ventricular myosin. Biochim. Biophys. Acta. 1979; 581: 283
   PubMedGoogle Scholar
• Fraser I. H., Gordon A. S., Liew C. C. Studies of nuclear proteins in the skeletal muscle of the cardiomyopathic Syrian hamster. J. Neurol. Sci. 1979; 42: 303
   PubMed Web of Science ®Google Scholar
• Liew C., Sole M. S. Nuclear proteins in the heart of the cardiomyopathic Syrian hamster. Phosphorylation of phenol-soluble non-histone proteins. Circ. Res. 1978; 42: 637
   PubMed Web of Science ®Google Scholar
• Liew C, Sole M. J., Silver M. D., Wigle E. D. Electrophoretic profiles of nonhistone nuclear proteins of human hearts with muscular subaortic stenosis. Circ. Res. 1980; 46: 513
   PubMedGoogle Scholar
• Brevet A., Whalen R. G. Comparative structural analysis of myosin after limited tryptic hydrolysis by use of two-dimensional gel electrophoresis. Biochemie 1978; 60: 459
   PubMed Web of Science ®Google Scholar
• Flink I. L., Rader J. H., Morkin E. Thyroid hormone stimulates synthesis of a cardiac myosin isozyme. J. Biol. Chem. 1979; 254: 3105
   PubMed Web of Science ®Google Scholar
• Tollaksen S. L., Edwards J. J., Anderson N. G. The use of carbamylated charge standards for testing batches of ampholytes used in two-dimensional electrophoresis. Electrophoresis 1981; 2: 155
   Web of Science ®Google Scholar
• Clark B. F. C. Towards a total human protein map. Nature (London) 1981; 292: 491
   PubMed Web of Science ®Google Scholar
• Giometti C. S., Anderson N. G., Tollaksen S. L., Edwards J. J., Anderson N. L. Analytical techniques for cell fractions. XXV11. Use of heart proteins as reference standards in two-dimensional electrophoresis. Anal. Biochem. 1980; 102: 47
   PubMed Web of Science ®Google Scholar
• Anderson N. L., Taylor J., Scandora A. E., Coulter B. P., Anderson N. G. The TYCHO system for computer analysis of two-dimensional gel electrophoresis patterns. Clin. Chem. 1981; 27: 1807
   PubMed Web of Science ®Google Scholar