Literature DB >> 7358630

Fluorometric studies on the light chains of skeletal muscle myosin. III. Effect of Ca2+ on the reactivity of two SH groups of DTNB light chain in myosin and in the isolated state.

K Yamamoto, R Honjo, T Sekine.   

Abstract

We studied the effect of Ca2+ on the reactivities of two SH groups of DTNB light chain (Cys 128 and Cys 157) using a fluorogenic thiol reagent. It was found that a Ca2+-induced change in reactivity occurred only with Cys 128 when the light chain was in an isolated state, whereas it occurred with both Cys 128 and Cys 157 when the light chain was incorporated in myosin. These results indicate that the Ca2+-induced change in the conformation of DTNB light chain in the isolated state was different from that of the light chain in myosin. It may therefore be difficult to relate the Ca2+-induced conformational change observed in the isolated DTNB light chain to the molecular mechanism of myosin-linked Ca2+ regulation.

Entities:  

Mesh:

Substances:

Year:  1980        PMID: 7358630     DOI: 10.1093/oxfordjournals.jbchem.a132727

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


  2 in total

1.  Orientation of spin-labeled light chain-2 exchanged onto myosin cross-bridges in glycerinated muscle fibers.

Authors:  B Hambly; K Franks; R Cooke
Journal:  Biophys J       Date:  1991-01       Impact factor: 4.033

2.  Influence of myosin heavy chains on the Ca2+-binding properties of light chain, LC2.

Authors:  S Srivastava; A Muhlrad; J Wikman-Coffelt
Journal:  Biochem J       Date:  1981-03-01       Impact factor: 3.857

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.