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Characterization of the interaction between human protein S and C4b-binding protein (C4bp).

Characterization of the interaction between human protein S and C4b-binding protein (C4bp). Research Abstract Details 

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  • Characterization of the interaction between human protein S and C4b-binding protein (C4bp). Abstract Text:

    m nukatsukaM Nukatsuka,s nagasawaS Nagasawa,

    C4b-binding protein, C4bp, is a regulatory factor of the complement system and is also known to be a binding protein of vitamin K-dependent coagulation factor, protein S. Whereas the C4b-binding site is known to be located in the middle part of the subunit chains of C4bp, the location and properties of protein S-binding site are uncertain. Therefore, we have examined the characteristics of the interaction between human protein S and C4bp. Proteolysis of C4bp-protein S complex with chymotrypsin yielded N-terminal-derived 48-kDa fragments of C4bp subunit chains and a C-terminal-derived 160-kDa core fragment of C4bp, to which protein S was still bound. This result suggested that the protein S-binding site is located in the core domain of C4bp. Gel filtration of guanidine-treated C4bp-protein S complex in the absence of guanidine resulted in the separation of C4bp and protein S. Binding assay with 125I-labeled protein S showed that the guanidine-treated C4bp lacked the protein S-binding activity. This result suggests that the protein S-binding site in C4bp is denatured irreversibly by guanidine treatment and therefore seems to be dependent on a specific conformation of C4bp. The C4bp-binding site of protein S was lost upon thrombin treatment, suggesting that the N-terminal thrombin-sensitive region of protein S may be related to the C4bp-binding site. Although free protein S was susceptible to chymotrypsin, leukocyte elastase, and cathepsin G, C4bp-bound protein S was found to be resistant to these proteases.(ABSTRACT TRUNCATED AT 250 WORDS)

    Characterization of the interaction between human protein S and C4b-binding protein (C4bp). Publishing Authors By Initials

    m nukatsukaM Nukatsuka,s nagasawaS Nagasawa,

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

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    Characterization of the interaction between human protein S and C4b-binding protein (C4bp). Journal Published:

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

    Journal: Journal of biochemistry

    VOLUME: 102

    Page Numbers: 599-605

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Sep

    YEAR: 1987

    Characterization of the interaction between human protein S and C4b-binding protein (C4bp). Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Characterization of the interaction between human protein S and C4b-binding protein (C4bp). Keywords Mesh Terms:

    KEYWORDS: Thrombin

    MESH TERMS: pharmacology

    Chemical & Substance for Abstract: Characterization of the interaction between human protein S and C4b-binding protein (C4bp). Information

    Substance Name: Thrombin

    Registry Number: EC 3.4.21.5

    Grant and Affiliation Information for Characterization of the interaction between human protein S and C4b-binding protein (C4bp).

    AFFILIATION: Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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