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Jens Christian Jensenius

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 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. / Poulsen, K; Krøll, J; Nielsen, A H; Jensenius, J; Malling, C; Jensenius, Jens Christian.

In: BBA General Subjects, Vol. 577, No. 1, 1979, p. 1-10.

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Author

Poulsen, K ; Krøll, J ; Nielsen, A H ; Jensenius, J ; Malling, C ; Jensenius, Jens Christian. / 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. In: BBA General Subjects. 1979 ; Vol. 577, No. 1. pp. 1-10.

Bibtex

@article{cc61b23019754fd4bc08485e7e16a084,
title = "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",
abstract = "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.",
keywords = "Animals, Blood Proteins, Carrier Proteins, Guanidines, Immunoelectrophoresis, Immunoelectrophoresis, Two-Dimensional, Lipoproteins, Mice, Molecular Weight, Nephrectomy, Protease Inhibitors, Protein Binding, Protein Conformation, Renin, Submandibular Gland",
author = "K Poulsen and J Kr{\o}ll and Nielsen, {A H} and J Jensenius and C Malling and Jensenius, {Jens Christian}",
year = "1979",
language = "English",
volume = "577",
pages = "1--10",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier BV",
number = "1",

}

RIS

TY - JOUR

T1 - 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

AU - Poulsen, K

AU - Krøll, J

AU - Nielsen, A H

AU - Jensenius, J

AU - Malling, C

AU - Jensenius, Jens Christian

PY - 1979

Y1 - 1979

N2 - 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.

AB - 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.

KW - Animals

KW - Blood Proteins

KW - Carrier Proteins

KW - Guanidines

KW - Immunoelectrophoresis

KW - Immunoelectrophoresis, Two-Dimensional

KW - Lipoproteins

KW - Mice

KW - Molecular Weight

KW - Nephrectomy

KW - Protease Inhibitors

KW - Protein Binding

KW - Protein Conformation

KW - Renin

KW - Submandibular Gland

M3 - Journal article

C2 - 427206

VL - 577

SP - 1

EP - 10

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 1

ER -