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Characterization of regulatory light chain-a myosin kinase from smooth muscle of scallop, Patinopecten yessoensis.

Characterization of regulatory light chain-a myosin kinase from smooth muscle of scallop, Patinopecten yessoensis. Research Abstract Details 

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  • Characterization of regulatory light chain-a myosin kinase from smooth muscle of scallop, Patinopecten yessoensis. Abstract Text:

    h sohmaH Sohma,f moritaF Morita,

    The protein kinase that phosphorylates the regulatory light chain-a (RLC-a) of scallop smooth muscle myosin was isolated from scallop smooth muscle (Sohma, H. & Morita, F. (1986) J. Biochem. 100, 1155-1163). The enzymatic properties of this kinase (aMK) were investigated using RLC-a as the substrate. The Km value for ATP was 6.5 microM in the presence of 27 microM RLC-a at pH 7.0, and that for RLC-a was 133 microM in the presence of 1 mM ATP. The Vm value at saturation of both RLC-a and ATP was 0.25 s-1 at pH 7.0. The pH activity curve for aMK was bell-shaped with a maximum at around pH 7.8. The aMK activity was inhibited strongly by an increase in the KCl concentration. aMK required Mg2+, but was inhibited by high concentrations of Mg2+. The optimum activity was seen at 3 mM MgCl2. The mode of inhibition of the aMK activity by Ca2+ was studied. Assuming that the binding of Ca2+ to aMK induces the inhibition, the dissociation constant of Ca2+ was estimated to be 64 microM. aMK also phosphorylated LC20 of chicken gizzard myosin at a similar rate to that for RLC-a and the DTNB light chain of rabbit skeletal muscle myosin at a more lower rate. The helix and beta-sheet contents of aMK were estimated to be 19 and 30%, respectively, from the CD spectrum.

    Characterization of regulatory light chain-a myosin kinase from smooth muscle of scallop, Patinopecten yessoensis. Publishing Authors By Initials

    h sohmaH Sohma,f moritaF Morita,

    For similar investigative techniques: chemistry, analytical: photometry: spectrophotometry: spectrophotometry, ultraviolet research abstracts see: investigative techniques: chemistry, analytical: photometry: spectrophotometry: spectrophotometry, ultraviolet research

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    Characterization of regulatory light chain-a myosin kinase from smooth muscle of scallop, Patinopecten yessoensis. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 101

    Page Numbers: 497-502

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Feb

    YEAR: 1987

    Characterization of regulatory light chain-a myosin kinase from smooth muscle of scallop, Patinopecten yessoensis. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Characterization of regulatory light chain-a myosin kinase from smooth muscle of scallop, Patinopecten yessoensis. Keywords Mesh Terms:

    KEYWORDS: Spectrophotometry, Ultraviolet

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Characterization of regulatory light chain-a myosin kinase from smooth muscle of scallop, Patinopecten yessoensis. Information

    Substance Name: Myosin-Light-Chain Kinase

    Registry Number: EC 2.7.1.117

    Grant and Affiliation Information for Characterization of regulatory light chain-a myosin kinase from smooth muscle of scallop, Patinopecten yessoensis.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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