Two-Site Direct Immunoassay Specific for Active Renin
نویسندگان
چکیده
منابع مشابه
Two-site direct immunoassay specific for active renin.
A sensitive immunoradiometric assay, without an enzymatic step and specific for active human renin, was developed with use of two monoclonal antibodies (MAbs). In this assay system, the first MAb was coupled to magnetic beads (Magnogel); the second one, directed against the active form of the enzyme, was radiolabeled with 125I. The specificity of this assay was demonstrated in experiments measu...
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Incubation of human plasma prorenin (PR), the enzymatically inactive precursor of renin (EC 3.4.23.15), with a number of nonpeptide high-affinity active site-directed renin inhibitors induces a conformational change in PR, which was detected by a monoclonal antibody that reacts with active renin but not with native inactive PR. This conformational change also occurred when inactive PR was activ...
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We have identified and characterized an anti-human renin monoclonal antibody R1-20-5 that is selective for human active renin. R1-20-5 binds active renin with a dissociation constant (Kd) of 2.5 x 10(-7) M/l and inhibits renin enzymatic activity with an inhibitory constant (IC50) of 1.4 x 10(-8) M/l. R1-20-5 competes with a synthetic renin inhibitor for binding with renin, demonstrating further...
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We developed a sensitive and specific heterogeneous enzyme immunoassay for measuring angiotensin I (AI) or renin (EC 3.4.99.19) activities. Linking AI under carefully controlled conditions by means of N-succinimidyl-3-(2-pyridyldithio)propionate to highly purified beta-D-galactosidase (EC 3.2.1.23) produced a well-defined conjugate in high yield. The procedure is simple and consists of three st...
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Electrostatic interactions are of vital importance in diverse aspects of protein structure and function [1-5], including the catalytic activity [6,7], ligand binding [8], complex formation [9], proton transport [10,11], as well as their stability of folded proteins [12,13]. These interactions involve full charges on the side chains of ionizable amino acids that arise from the association and di...
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ژورنال
عنوان ژورنال: Clinical Chemistry
سال: 1992
ISSN: 0009-9147,1530-8561
DOI: 10.1093/clinchem/38.10.1959