Alkali light chains are involved in stabilization of myosin head

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

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


1. 1. Fast skeletal myosin subfragment 1 (S1) was separated into two isozymes, S1(A1) and S1(A2), based on the associated alkali light chain, and their thermostabilities were compared. 2. 2. Inactivation rate constants of Ca2+-ATPase (at 30 and 35°C) were higher and heat-induced turbidity increase at 340 nm (at 40°C) was faster with S1(A1) than with S1(A2), indicating a higher stability of S1(A2). 3. 3. When S1 isozymes were incubated in the presence of excess alkali light chain, turbidity increase was markedly reduced, depending on the amount of light chain added. 4. 4. Results obtained strongly suggest that alkali light chains are involved in the maintenance of myosin head structure.

Original languageEnglish
Pages (from-to)1097-1103
Number of pages7
JournalInternational Journal of Biochemistry
Issue number10
Publication statusPublished - 1990
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry


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