Effects of anti-LMM antibodies on the solubility of chicken skeletal muscle myosin

Macdonald Wick, Fern Tablin, Everett Bandman

Research output: Contribution to journalArticle

6 Scopus citations


Monoclonal antibody Fab fragments which bind epitopes in the rod domain of skeletal muscle myosin had specific effects on the solubility properties of chicken muscle myosin in vitro. Two antibodies (NA4 and 5C3), which bind at the C-terminal portion of the rod domain caused myosin to remain soluble and monomeric in 0.1 M KCl, pH 7.2, conditions in which myosin normally aggregates into filamentous structures. Other antibodies (EB165 and AB8), which bind in the middle of the rod did not alter either myosin solubility or the morphology of the myosin assemblies formed. These results demonstrate the importance of the C-terminus of the myosin rod as a domain involved in regulating myosin interactions and solubility.

Original languageEnglish (US)
Pages (from-to)379-395
Number of pages17
JournalJournal of Food Biochemistry
Issue number5
StatePublished - 1997


ASJC Scopus subject areas

  • Food Science
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

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