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Renin binding proteins in plasma. Binding of renin to some of the plasma protease inhibitors, to lipoproteins, and to a non-trypsin-binding unidentified plasma protein

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Renin is found in mouse plasma as high molecular weight forms, in addition to the fully active 40 000 dalton form. By using freshly 125 I-labelled 40 000 dalton pure submaxillary mouse renin, no binding to plasma proteins was demonstrable. However, unfolding and refolding of the labelled renin by guanidine facilitated binding to specific mouse and human plasma proteins. By using antibodies against individual human plasma proteins, the specific binding proteins were identified to be the plasma protease inhibitors: alpha2-macroglobulin, inter-alpha-trypsin inhibitor, alpha2-antithrombin. Binding was also demonstrated to alpha1- and beta1-lipoproteins, albumin and to a non trypsin binding unidentified plasma protein. No binding to 56 other tested proteins was demonstrable. It is concluded that the native 40 000 renin does not bind, but that a conformational change of the renin molecule most likely is necessary before binding occurs. It is discussed whether or not inactive or high molecular weight forms of renin in plasma are 40 000 renin bound to plasma protease inhibitors and lipoprotein.
Original languageEnglish
JournalBBA General Subjects
Volume577
Issue1
Pages (from-to)1-10
Number of pages10
ISSN0304-4165
Publication statusPublished - 1979

    Research areas

  • Animals, Blood Proteins, Carrier Proteins, Guanidines, Immunoelectrophoresis, Immunoelectrophoresis, Two-Dimensional, Lipoproteins, Mice, Molecular Weight, Nephrectomy, Protease Inhibitors, Protein Binding, Protein Conformation, Renin, Submandibular Gland

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