Structural and functional changes of myosin during development: comparison with adult fast, slow and cardiac myosin. |
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Authors: | F A Sréter M Bálint J Gergely |
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Institution: | 1. Department of Muscle Research, Boston Biomedical Research Institute, Boston, Massachusetts 02114 USA;2. Department of Neurology, Massachusetts General Hospital, Boston, Massachusetts 02114 USA;3. Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts 02114 USA |
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Abstract: | ATPase (Ca2+ and K+ activated) activity of myosin prepared from muscles of 3–4 week rabbit embryos (EM) is slighly lower than that of adult fast muscle myosin (FM), but in contrast to the less active adult slow muscle myosin (SM) is stable on exposure to pH 9.2. Studies of the time course, by means of Na dodecyl-SO4 polyacrylamide gel electrophoresis, of changes in the pattern of polypeptides released by tryptic digestion show that in this regard EM is closest to SM. The light chain complement of EM appears identical with that of FM rather than of SM or cardiac myosin (CM) by the criteria of coelectrophoresis and removal by 5,5′-dithio-2-dinitrobenzoate treatment of LC2 except that the relative amount of LC3 is less in EM than in FM. The staining pattern of light meromyosin (EMM) paracrystals prepared from EM is distinct from either the FM, SM or CM LMM staining pattern. These studies suggest that different genes are involved in the coding for embryonic and adult heavy chains. |
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Keywords: | light chain 1 light chain 2 light chain 3 HMM heavy meromyosin LMM light meromyosin EM embryonic muscle SM slow myosin FM fast myosin CM cardiac myosin SDS sodium dodecyl sulfate DTNB 5 5′-dithiobis-(2-nitrobenzoic acid) EDTA ethylenediamine tetraacetic acid DTT dithiothreitol SPAGE SDS polyacrylamide gel electrophoresis |
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