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Partial purification and characterization of exudate gelatinase in the acute phase of carrageenin-induced inflammation in rats.

Partial purification and characterization of exudate gelatinase in the acute phase of carrageenin-induced inflammation in rats. Research Abstract Details 

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  • Partial purification and characterization of exudate gelatinase in the acute phase of carrageenin-induced inflammation in rats. Abstract Text:

    h nakagawaH Nakagawa,k sakataK Sakata,

    Gelatinase has been partially purified from exudate in the acute phase of carrageenin-induced inflammation in rats. The enzyme occurs in a latent form that can be activated with 4-aminophenylmercuric acetate (APMA). The latent gelatinase was separated into an active gelatinase and a protein fraction by zinc-chelating Sepharose 6B column chromatography in the final step of purification, suggesting that the latent gelatinase is an enzyme-inhibitor complex. The pH optimum of the active gelatinase is about 7.5 and no reactivity toward native type I collagen or alpha-casein was detected. The molecular weights of the latent and active gelatinases were about 245,000 and about 185,000, respectively, as determined by gel filtration on Sephadex G-200. On the other hand, both latent and active gelatinases occurred in multiple forms in SDS-substrate polyacrylamide gel electrophoresis; the latent gelatinase showed two bands with molecular weights of 105,000 and 69,000, and two additional bands of 88,000 and 83,000 appeared when the latent gelatinase was activated with APMA, while the active gelatinase showed all four species. The active gelatinase was inhibited by metallo-proteinase inhibitors, but not by serine- or cysteine-proteinase inhibitors, suggesting that the exudate gelatinase is a metallo-proteinase. The active gelatinase was also inhibited by serum proteins such as albumin and gamma-globulin, suggesting that gelatinase does not remain in an active form in the inflammatory lesion, where the vascular permeability is increased.

    Partial purification and characterization of exudate gelatinase in the acute phase of carrageenin-induced inflammation in rats. Publishing Authors By Initials

    h nakagawaH Nakagawa,k sakataK Sakata,

    For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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    Partial purification and characterization of exudate gelatinase in the acute phase of carrageenin-induced inflammation in rats. Journal Published:

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

    Journal: Journal of biochemistry

    VOLUME: 100

    Page Numbers: 1499-506

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Dec

    YEAR: 1986

    Partial purification and characterization of exudate gelatinase in the acute phase of carrageenin-induced inflammation in rats. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Partial purification and characterization of exudate gelatinase in the acute phase of carrageenin-induced inflammation in rats. Keywords Mesh Terms:

    KEYWORDS: Substrate Specificity

    MESH TERMS: isolation & purification

    Chemical & Substance for Abstract: Partial purification and characterization of exudate gelatinase in the acute phase of carrageenin-induced inflammation in rats. Information

    Substance Name: Gelatinases

    Registry Number: EC 3.4.24.-

    Grant and Affiliation Information for Partial purification and characterization of exudate gelatinase in the acute phase of carrageenin-induced inflammation in rats.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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