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PMID: 7287900 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Myosin light chains of avian and mammalian slow muscles: evidence of intraspecific polymorphism.

Journal of muscle research and cell motility ·Vol. 2 ·No. 3 ·1981-09-00 ·Pages 335-42

Carraro U, dalla Libera L, Catani C

Abstract

The myosin light chains of slow muscles from different species have been examined two-dimensional gel electrophoresis. While the myosin light chain 2S of mammalian soleus muscles (rabbit, rat and guinea-pig) could not be distinguished from that of avian anterior latissimus dorsi (chicken and turkey), the 1S light chain complement of myosins shows inter- and intraspecific differences. The 1S light chain varies between birds and mammals. The 1S light chain is absent in avian slow myosins and has an electrophoretic mobility peculiar to each mammalian species. Furthermore the relative amount of 1S and 1S light chains varies in different muscles of the same mammalian species and among species.

MeSH Terms
Actins/metabolism Actomyosin/metabolism Animals Chemical Phenomena Chemistry Chickens Diaphragm Electrophoresis, Polyacrylamide Gel Guinea Pigs Muscles/metabolism Myosins/metabolism Rabbits Rats Species Specificity Tropomyosin/metabolism Turkeys
Chemicals
Actins Tropomyosin Actomyosin Myosins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Carraro U
dalla Libera L
Catani C
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25 references, click to expand
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Article Info
Journal
Journal of muscle research and cell motility
Abbr.
J Muscle Res Cell Motil
ISSN
0142-4319
DOI
10.1007/BF00713271
Published
1981-09-00
Pages
335-42
Language
English
Region
Netherlands
NLM ID
8006298
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00713271 View journal details
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