
Cardiac and skeletal muscle myosin polymorphism
Author(s) -
Susan Lowey
Publication year - 1986
Publication title -
medicine and science in sports and exercise
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.703
H-Index - 224
eISSN - 1530-0315
pISSN - 0195-9131
DOI - 10.1249/00005768-198606000-00006
Subject(s) - myosin , isozyme , skeletal muscle , myh7 , biology , pectoralis muscle , cardiac muscle , myosin light chain kinase , pectoralis major muscle , enzyme , anatomy , biochemistry
Skeletal muscles, unlike cardiac tissue, express several myosin isozymes during development which differ in primary structure from adult myosin. Monoclonal antibodies have shown the presence of at least two embryonic myosins, followed by a post-hatch myosin that persists until the appearance of adult myosin in chicken pectoralis muscle. Although the two major cardiac isozymes differ in enzymatic activity, the avian skeletal myosin isozymes all share the same high level of ATPase activity found for adult pectoralis myosin. The functional basis for the extensive myosin polymorphism in skeletal muscles thus remains to be determined.