Possible presence of the difference peptide in alkali light chain 1 of fish fast skeletal myosin

Y. Ochiai, T. Kobayashi, A. Handa, S. Watabe, K. Hashimoto

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9 Citations (Scopus)

Abstract

1. 1. Presence of N-terminal peptide ("difference peptide") in alkali light chain 1 (A1) of fish fast skeletal myosin was examined by comparing two kinds of light chain-based myosin subfragment 1 (S1) isozymes from the yellowtail Seriola quinqueradiata. 2. 2. On tryptic digestion, A1 was cleaved to a smaller fragment (mol. wt decrement by 2000) along with the cleavage of S1 heavy chain, while A2 was resistant to trypsin. Two-dimensional gel electrophoresis showed that A1 released a basic peptide by tryptic digestion. 3. 3. Both S1 isozymes showed clear kinetic differences in actin-activated Mg-ATPase activity, suggesting a higher affinity of A1 for actin. Affinity of A2 for heavy chain was also estimated to be about 2-fold higher than that of A1, as judged by the model experiments in which rabbit S1 isozymes were hybridized with heterologous alkali light chains.

Original languageEnglish
Pages (from-to)793-801
Number of pages9
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume97
Issue number4
DOIs
Publication statusPublished - 1990

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology

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