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Azuki bean (Vigna angularis) protease inhibitors: isolation and amino acid sequences.

Azuki bean (Vigna angularis) protease inhibitors: isolation and amino acid sequences. Research Abstract Details 

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  • Azuki bean (Vigna angularis) protease inhibitors: isolation and amino acid sequences. Abstract Text:

    c ishikawaC Ishikawa,k watanabeK Watanabe,n sakataN Sakata,c nakagakiC Nakagaki,s nakamuraS Nakamura,k takahashiK Takahashi,

    Double-headed protease inhibitors I, IIa, and IIc (AB I, AB IIa, and AB IIc) have been purified from azuki beans "Takara" (Vigna angularis) by conventional chromatographic methods and their amino acid sequences have been determined. AB I, AB IIa, and AB IIc had molecular weights of 9,166, 8,661, and 8,756 daltons, consisting of 82, 78, 79 amino acid residues, respectively. The molecular weights of these inhibitors, determined by gel filtration at pH 8.0, were 18,000 for AB I and 17,000 for both AB IIa and AB IIc, indicating that the inhibitors are dimers. The inhibitors had isoelectric points of 4.7 (AB I), 6.8 (AB IIa), and 6.2 (AB IIc). AB I stoichiometrically inhibited both trypsin and chymotrypsin at a molar ratio of 1 : 1. On the other hand, AB IIa and AB IIc both inhibited trypsin at a molar ratio of about 1 : 2 and also inhibited chymotrypsin, though only weakly. Sequence comparison with other double-headed inhibitors indicated the reactive sites of AB IIa and AB IIc for trypsin to be Lys26-Ser27 and Arg53-Ser54, and those of AB I for trypsin and chymotrypsin to be Lys26-Ser27 and Tyr53-Ser54, respectively. The differences between AB IIa and AB IIc were that AB IIa lacked the C-terminal aspartic acid residue, and that Glu10 and Arg60 in AB IIa were replaced by Gln10 and His60 in AB IIc. A comparison between AB IIa and AB I revealed 25 variant amino acids among the 78 residues of AB IIa; further, Ab IIa lacked 4 amino acid residues in the C-terminal region of AB I.

    Azuki bean (Vigna angularis) protease inhibitors: isolation and amino acid sequences. Publishing Authors By Initials

    c ishikawaC Ishikawa,k watanabeK Watanabe,n sakataN Sakata,c nakagakiC Nakagaki,s nakamuraS Nakamura,k takahashiK Takahashi,

    For similar chemical actions and uses: pharmacologic actions: molecular mechanisms of pharmacological action: enzyme inhibitors: protease inhibitors: serine proteinase inhibitors: trypsin inhibitors research abstracts see: chemical actions and uses: pharmacologic actions: molecular mechanisms of pharmacological action: enzyme inhibitors: protease inhibitors: serine proteinase inhibitors: trypsin inhibitors research

    PUBMED ID PMID:

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    Azuki bean (Vigna angularis) protease inhibitors: isolation and amino acid sequences. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 97

    Page Numbers: 55-70

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Jan

    YEAR: 1985

    Azuki bean (Vigna angularis) protease inhibitors: isolation and amino acid sequences. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Azuki bean (Vigna angularis) protease inhibitors: isolation and amino acid sequences. Keywords Mesh Terms:

    KEYWORDS: Trypsin Inhibitors

    MESH TERMS: isolation & purification

    Chemical & Substance for Abstract: Azuki bean (Vigna angularis) protease inhibitors: isolation and amino acid sequences. Information

    Substance Name: auR protein, Staphylococcus aureus

    Registry Number: EC 3.4.24.29

    Grant and Affiliation Information for Azuki bean (Vigna angularis) protease inhibitors: isolation and amino acid sequences.

    AFFILIATION:

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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