Open AccessContractile protein isozymes in muscle development: identification of an embryonic form of myosin heavy chain.
Author(s) -
Robert G. Whalen,
Ketty Schwartz,
P. Bouveret,
Susan M. Sell,
François Gros
Publication year - 1979
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.76.10.5197
Subject(s) - myosin , isozyme , embryonic stem cell , biochemistry , biology , meromyosin , cleavage (geology) , myosin light chain kinase , embryogenesis , muscle tissue , myocyte , microbiology and biotechnology , chemistry , myosin head , enzyme , anatomy , gene , paleontology , fracture (geology)
The nature of the myosin heavy chain in embryonic muscle tissue, cultured muscle cells, and several adult muscles was investigated. After denaturation with sodium dodecyl sulfate, purified rat myosins were subjected to partial proteolytic cleavage or immunological analysis using microcomplement fixation. Three types of myosin heavy chains could be demonstrated by both approaches. Whereas adult muscles contain fast- or slow-type myosin heavy chains, embryonic tissue and cultured muscle cells harbor a distinct embryonic form. The existence of this distinct form further characterizes the isozymic transitions of contractile proteins during muscle development.