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Amino acid sequence studies on cyanogen bromide peptides of chicken caldesmon which bind to calmodulin.

Amino acid sequence studies on cyanogen bromide peptides of chicken caldesmon which bind to calmodulin. Research Abstract Details 

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  • Amino acid sequence studies on cyanogen bromide peptides of chicken caldesmon which bind to calmodulin. Abstract Text:

    t takagiT Takagi,m yazawaM Yazawa,t uenoT Ueno,s suzukiS Suzuki,k yagiK Yagi,

    Three major calmodulin-binding cyanogen bromide peptides (fragments A, B, and D) were isolated from chicken gizzard muscle caldesmon and their amino acid sequences were determined. The molecular masses of fragments A, B, and D were estimated to 16, 12, and 9 kDa, respectively, by SDS-urea polyacrylamide gel electrophoresis. Fragment A was composed of 102 amino acid residues and contained homoserine at the C terminus. The amino acid sequence from the 37th residue of fragment A corresponds to the N-terminal sequence of the 15 kDa peptide which was obtained by thrombin digestion [Mornet, D., Audemard, E., & Derancourt, J. (1988) Biochem. Biophys. Res. Commun. 154, 564-571]. Thrombin 15 kDa peptide binds to F-actin but does not bind to calmodulin. Thus the N-terminal 36 residues and the C-terminal part from the 37th residue of fragment A are supposed to bind to calmodulin and F-actin, respectively. The sequences of fragments B and D were identical, but fragment D was composed of 64 amino acid residues and ended with tryptophan, whereas fragment B was of 98 or 99 amino acid residues and ended with proline. Both fragments B and D are supposed to be the C-terminal peptides of chicken caldesmon. Fragment B had heterogeneous sequences at the C-terminal region. These results can explain the reported heterogeneity of chicken caldesmon in charge and molecular mass.

    Amino acid sequence studies on cyanogen bromide peptides of chicken caldesmon which bind to calmodulin. Publishing Authors By Initials

    t takagiT Takagi,m yazawaM Yazawa,t uenoT Ueno,s suzukiS Suzuki,k yagiK Yagi,

    For similar enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases research abstracts see: enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases research

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    Amino acid sequence studies on cyanogen bromide peptides of chicken caldesmon which bind to calmodulin. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 106

    Page Numbers: 778-83

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Nov

    YEAR: 1989

    Amino acid sequence studies on cyanogen bromide peptides of chicken caldesmon which bind to calmodulin. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Amino acid sequence studies on cyanogen bromide peptides of chicken caldesmon which bind to calmodulin. Keywords Mesh Terms:

    KEYWORDS: Serine Endopeptidases

    MESH TERMS: analysis

    Chemical & Substance for Abstract: Amino acid sequence studies on cyanogen bromide peptides of chicken caldesmon which bind to calmodulin. Information

    Substance Name: lysyl endopeptidase

    Registry Number: EC 3.4.21.50

    Grant and Affiliation Information for Amino acid sequence studies on cyanogen bromide peptides of chicken caldesmon which bind to calmodulin.

    AFFILIATION: Biological Institute, Faculty of Science, Tohoku University, Miyagi.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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