Literature DB >> 2722761

Ca2+-sensitive transition in the molecular conformation of molluscan muscle myosins.

M Takahashi1, Y Fukushima, K Inoue, Y Hasegawa, F Morita, K Takahashi.   

Abstract

Filament assemblies of myosin molecules purified from scallop adductor muscles were stabilized by Ca2+ in the presence of ATP or ADP. Electron micrographs showed that the tail part of monomeric myosin molecules was folded in the absence of Ca2+, but was extended in the presence of Ca2+ at physiological ionic strength.

Entities:  

Mesh:

Substances:

Year:  1989        PMID: 2722761     DOI: 10.1093/oxfordjournals.jbchem.a122628

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  3 in total

Review 1.  Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.

Authors:  Scott L Hooper; Kevin H Hobbs; Jeffrey B Thuma
Journal:  Prog Neurobiol       Date:  2008-06-20       Impact factor: 11.685

2.  The calcium ion dependence of scallop myosin ATPase activity.

Authors:  A R Walmsley; G E Evans; C R Bagshaw
Journal:  J Muscle Res Cell Motil       Date:  1990-12       Impact factor: 2.698

3.  Myorod, a thick filament protein in molluscan smooth muscles: isolation, polymerization and interaction with myosin.

Authors:  N Shelud'ko; T Permjakova; K Tuturova; O Neverkina; A Drozdov
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.