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Studies on the serine proteases associated with rat liver chromatin.

Studies on the serine proteases associated with rat liver chromatin. Research Abstract Details 

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  • Studies on the serine proteases associated with rat liver chromatin. Abstract Text:

    k tsurugiK Tsurugi,k ogataK Ogata,

    The chromatin fraction of rat liver exhibited proteolytic activity caused by serine proteases, with maximal activity at pH 8 or 10. They were analyzed by affinity labeling with [3H]diisopropylfluorophosphate followed by SDS-polyacrylamide gel electrophoresis, and partially purified by gel filtration through Sepharose 6B after selective extraction from the chromatin fraction. The following results were obtained. 1. The chromatin fraction contained three DFP-binding proteins with molecular weights of 52,000, 25,000, and 15,000 daltons, and they were tentatively designated proteins A, B, and C, respectively. Unlike proteins A and B, protein C reacted with DFP more strongly at pH 10 than at pH 8. A greater part of protein B was present in the nucleoli, while the others were predominantly distributed in extra-nucleolar chromatin. 2. Proteins A and B were extracted from the chromatin fraction by 5 M urea and 0.7 M NaCl, respectively; while protein C was not extractable by either solution. Proteins A and B were further purified by gel filtration through Sepharose 6B. 3. Protein B was a neutral protease with a maximal activity for 3H-labeled ribosomal proteins at pH 8 and showed high specificity for basic proteins, such as histone and ribosomal proteins. Protein A was an alkaline protease with a maximal activity at pH 10 and showed proteolytic activity not only for basic proteins but also for hydrophobic proteins, such as casein and non-histone proteins of chromatin. 4. Protein A was activated at pH 8 by high concentrations of NaCl, suggesting the presence of some inhibitor(s). Protein A was converted to protein C at pH 10, and also at pH 8 with high concentrations of NaCl. Thus, protein A is suggested to be the complex of protein C and unknown inhibitor(s). 5. When the chromatin fraction was incubated at pH 10, non-histone proteins were degraded much faster than at pH 8, although H1 histone was degraded at similar rates at both pHs. These results indicate that the chromatin fraction of rat liver contains at least two kinds of serine proteases, B and C, and that protease B is probably involved in the metabolism of basic protein, especially H1 histone. Protease C, the greater part of which associates with some inhibitors to form protein A, may play its main role in the metabolism of non-histone proteins.

    Studies on the serine proteases associated with rat liver chromatin. Publishing Authors By Initials

    k tsurugiK Tsurugi,k ogataK Ogata,

    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

    PUBMED ID PMID:

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    Studies on the serine proteases associated with rat liver chromatin. Journal Published:

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

    Journal: Journal of biochemistry

    VOLUME: 92

    Page Numbers: 1369-81

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Nov

    YEAR: 1982

    Studies on the serine proteases associated with rat liver chromatin. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Studies on the serine proteases associated with rat liver chromatin. Keywords Mesh Terms:

    KEYWORDS: Serine Endopeptidases

    MESH TERMS: pharmacology

    Chemical & Substance for Abstract: Studies on the serine proteases associated with rat liver chromatin. Information

    Substance Name: Serine Endopeptidases

    Registry Number: EC 3.4.21.-

    Grant and Affiliation Information for Studies on the serine proteases associated with rat liver chromatin.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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