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Characterization of monoclonal antibodies against human prorenin profragment and identification of active prorenins in plasma.

Characterization of monoclonal antibodies against human prorenin profragment and identification of active prorenins in plasma. Research Abstract Details 

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  • Characterization of monoclonal antibodies against human prorenin profragment and identification of active prorenins in plasma. Abstract Text:

    y ishizukaY Ishizuka,s iizumiS Iizumi,f akiyamaF Akiyama,h horiH Hori,r a poormanR A Poorman,t j loblT J Lobl,k murakamiK Murakami,

    Monoclonal antibodies were raised against a synthetic peptide (43 amino acid residues) that corresponds to the complete profragment of human prorenin. Seven monoclonal antibodies were chosen for further characterization. Two antibodies, 2-X-C1 and 4-X-E1, reacted with the middle region and C-terminus of the profragment and were isotyped IgG1. The affinity constants of these antibodies against the human profragment were 7.6 x 10(8) and 3.0 x 10(7) M-1, respectively. Immunoaffinity columns containing the antibodies 2-X-C1 and 4-X-E1, respectively, were used for the characterization of active prorenin in human plasma. This active prorenin strongly bound to the 4-X-E1 column and eluted as two separate peaks which corresponded to fully and partially active prorenin, respectively. The partially active prorenin had higher activity with a small substrate, tridecapeptide, than with a large one, angiotensinogen, although the fully active prorenin had the same renin activity irrespective of the size of the substrate. These data suggest that new forms of prorenin, active prorenin, exist in human plasma and that their active sites are completely or partially exposed to the substrates. Moreover, the active prorenin in plasma was found not only in human but also in all tested mammalians. Cross-reactivity among the profragments of mammalian plasma prorenins can be explained by conservation of the amino acid sequence (epitope) of the combining site.

    Characterization of monoclonal antibodies against human prorenin profragment and identification of active prorenins in plasma. Publishing Authors By Initials

    y ishizukaY Ishizuka,s iizumiS Iizumi,f akiyamaF Akiyama,h horiH Hori,ra poormanRA Poorman,tj loblTJ Lobl,k murakamiK Murakami,

    For similar enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: aspartic endopeptidases: renin research abstracts see: enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: aspartic endopeptidases: renin research

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    Characterization of monoclonal antibodies against human prorenin profragment and identification of active prorenins in plasma. Journal Published:

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

    Journal: Journal of biochemistry

    VOLUME: 106

    Page Numbers: 430-5

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Sep

    YEAR: 1989

    Characterization of monoclonal antibodies against human prorenin profragment and identification of active prorenins in plasma. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Characterization of monoclonal antibodies against human prorenin profragment and identification of active prorenins in plasma. Keywords Mesh Terms:

    KEYWORDS: Renin

    MESH TERMS: immunology

    Chemical & Substance for Abstract: Characterization of monoclonal antibodies against human prorenin profragment and identification of active prorenins in plasma. Information

    Substance Name: Renin

    Registry Number: EC 3.4.23.15

    Grant and Affiliation Information for Characterization of monoclonal antibodies against human prorenin profragment and identification of active prorenins in plasma.

    AFFILIATION: Institute of Applied Biochemistry, University of Tsukuba, Ibaraki.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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