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Electrophoretic separation by an improved method of fast myosin HCIIb-,HCIId-, and HCIIa-based isomyosins with specific alkali light chain combinations
An improved method of electrophoresis under nondenaturing conditions separated three electrophoretically distinct isomyosin triplets when applied to rat fast-twitch muscles displaying a predominance of one of the fast myosin heavy chain HCIIb, HCIId or HCIIa. The three isomyosin triplets, named FM1b...
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Published in: | FEBS letters 1990-11, Vol.275 (1), p.165-167 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | An improved method of electrophoresis under nondenaturing conditions separated three electrophoretically distinct isomyosin triplets when applied to rat fast-twitch muscles displaying a predominance of one of the fast myosin heavy chain HCIIb, HCIId or HCIIa. The three isomyosin triplets, named FM1b-FM3b, FM1d-FM3d, FM1a-FM3a, correspond to the three possible alkali light chain (I.C.) combinations (L.C.??? homodimer, LC??? LC3f heterodimer, and LC3f homodimer) with each fast HC isoform. Different proportions of these various isomyosins suggested specific affinities of light chains LC??? and LC3f for the fast heavy chain isoforms. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(90)81463-X |