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Comparative studies on actins from various sources. Fragments of actins from Ascaris muscle cleaved at cysteinyl residues in comparison with those of other actins.

Comparative studies on actins from various sources. Fragments of actins from Ascaris muscle cleaved at cysteinyl residues in comparison with those of other actins. Research Abstract Details 

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  • Comparative studies on actins from various sources. Fragments of actins from Ascaris muscle cleaved at cysteinyl residues in comparison with those of other actins. Abstract Text:

    t nakamuraT Nakamura,m yamaguchiM Yamaguchi,t yanagisawaT Yanagisawa,

    Pure actins were obtained from various animal muscles: Vertebrata (skeletal, smooth, and cardiac muscles), Prochordata (smooth muscle), Nematoda (obliquely striated muscle), and Mollusca (striated, smooth and obliquely striated muscles). These actins were all identical in apparent molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. All actins treated with 2-nitro-5-thiocyanobenzoic acid yielded four major (about 33,000, 26,000, 24,000, and less than 10,000 daltons) and three minor (22,000, 17,000, and 10,000 daltons) bands in addition to intact actin on gel electrophoresis. The results suggest that all actins from various types of muscle have cysteinyl residues at similar positions on the primary structure.

    Comparative studies on actins from various sources. Fragments of actins from Ascaris muscle cleaved at cysteinyl residues in comparison with those of other actins. Publishing Authors By Initials

    t nakamuraT Nakamura,m yamaguchiM Yamaguchi,t yanagisawaT Yanagisawa,

    For similar peptides: peptide fragments research abstracts see: peptides: peptide fragments research

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    Comparative studies on actins from various sources. Fragments of actins from Ascaris muscle cleaved at cysteinyl residues in comparison with those of other actins. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 85

    Page Numbers: 627-31

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Mar

    YEAR: 1979

    Comparative studies on actins from various sources. Fragments of actins from Ascaris muscle cleaved at cysteinyl residues in comparison with those of other actins. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Comparative studies on actins from various sources. Fragments of actins from Ascaris muscle cleaved at cysteinyl residues in comparison with those of other actins. Keywords Mesh Terms:

    KEYWORDS: Peptide Fragments

    MESH TERMS: analysis

    Chemical & Substance for Abstract: Comparative studies on actins from various sources. Fragments of actins from Ascaris muscle cleaved at cysteinyl residues in comparison with those of other actins. Information

    Substance Name: Cysteine

    Registry Number: 52-90-4

    Grant and Affiliation Information for Comparative studies on actins from various sources. Fragments of actins from Ascaris muscle cleaved at cysteinyl residues in comparison with those of other actins.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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    Comparative studies on actins from various sources Fragments of actins from Ascaris muscle cleaved at cysteinyl residues in comparison with those of other actins Related Publications

     

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