Comparison of adult, embryonic, and dystrophic myosin heavy chains from chicken muscle by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and peptide mapping.
作者： J. I. Rushbrook , A. Stracher
关键词: Sodium dodecyl sulfate 、 Polyacrylamide gel electrophoresis 、 Molecular biology 、 Peptide mapping 、 Myosin 、 Peptide 、 White (mutation) 、 Electrophoresis 、 Chemistry 、 Embryonic stem cell 、 Multidisciplinary
摘要: Abstract Chicken myosin heavy chains from adult fast white muscle fibers (both normal and dystrophic), slow red fibers, embryonic presumptive were compared by sodium dodecyl sulfate/polyacrylamide gel electrophoresis peptide mapping. The chain of migrated electrophoretically more slowly than the other myosins differed markedly them in its maps. dystrophic was similar to counterpart mapping but showed slight differences. map had general features that white, not red, contained definite differences former. results are consistent with existence a separate gene for myosin.
core.ac.uk
harvard.edu
highwire.org参考文章(26)
Tomoh MASAKI, Immunochemical comparison of myosins from chicken cardiac, fast white, slow red, and smooth muscle. Journal of Biochemistry. ,vol. 76, pp. 441- 449 ,(1974) , 10.1093/OXFORDJOURNALS.JBCHEM.A130586
Peter DEHM, Bjorn R. OLSEN, Darwin J. PROCKOP, Antibodies to Chick‐Tendon Procollagen FEBS Journal. ,vol. 46, pp. 107- 116 ,(1974) , 10.1111/J.1432-1033.1974.TB03602.X
A. Lewis Farr, Oliver H. Lowry, Rose J. Randall, Nira J. Rosebrough, Protein Measurement with the Folin Phenol Reagent Journal of Biological Chemistry. ,vol. 193, pp. 265- 275 ,(1951)
Genji Matsuda, Yoji Suzuyama, Tetsuo Maita, Toshiyo Umegane, The L-2 light chain of chicken skeletal muscle myosin. FEBS Letters. ,vol. 84, pp. 53- 56 ,(1977) , 10.1016/0014-5793(77)81055-7
F. Sreter, S. Holtzer, J. Gergely, H. Holtzer, Some properties of embryonic myosin. Journal of Cell Biology. ,vol. 55, pp. 586- 594 ,(1972) , 10.1083/JCB.55.3.586
GF Gauthier, S Lowey, Polymorphism of myosin among skeletal muscle fiber types. Journal of Cell Biology. ,vol. 74, pp. 760- 779 ,(1977) , 10.1083/JCB.74.3.760
G. HUSZAR, Developmental changes of the primary structure and histidine methylation in rabbit skeletal muscle myosin. Nature. ,vol. 240, pp. 260- 264 ,(1972) , 10.1038/NEWBIO240260A0
NEAL A. RUBINSTEIN, HOWARD HOLTZER, Fast and slow muscles in tissue culture synthesise only fast myosin Nature. ,vol. 280, pp. 323- 325 ,(1979) , 10.1038/280323A0
H. P. Hoffmann, B. R. Olsen, H. T. Chen, D. J. Prockop, Segment-long-spacing aggregates and isolation of COOH-terminal peptides from type I procollagen. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 73, pp. 4304- 4308 ,(1976) , 10.1073/PNAS.73.12.4304
J. F. Y. HOH, G. P. S. YEOH, Rabbit skeletal myosin isoenzymes from fetal, fast-twitch and slow-twitch muscles Nature. ,vol. 280, pp. 321- 323 ,(1979) , 10.1038/280321A0