Immunochemical studies of plasma kallikrein

The Journal of Clinical Investigation
A BagdasarianR W Colman


A monospecific antibody against human plasma kallikrein has been prepared in rabbits with kallikrein further purified to remove gamma globulins. The antisera produced contained antikallikrein and also anti-IgG, in spite of only 8% contamination of kallikrein preparation with IgG. The latter antibody was removed by adsorption of antisera with either Fletcher factor-deficient plasma or with purified IgG. Both kallikrein and prekallikrein (in plasma) cross-react with the antibody with no apparent difference between the precipitation arcs developed during immunoelectrophoresis and no significant difference in reactivity when quantified by radial immunodiffusion. Kallikrein antibody partially inhibits the esterolytic and fully inhibits the proteolytic activity of kallikrein. In addition, the antibody inhibits the activation of prekallikrein, as measured by esterase or kinin release. The magnitude of the inhibition is related to the molecular weight of the activator used. Thus, for the four activators tested, the greatest inhibition is observed with kaolin and factor XII(A), while large activator and the low molecular weight prekallikrein activators are less inhibited. With the kallikrein antibody, the incubation of kallikrein with e...Continue Reading


Aug 1, 1970·The Journal of Experimental Medicine·P C Harpel
Sep 1, 1971·Scandinavian Journal of Clinical and Laboratory Investigation·K Ohlsson
Jul 1, 1972·The Journal of Clinical Investigation·D J McConnell
Jun 1, 1973·The Journal of Clinical Investigation·A D SchreiberK F Austen
Feb 1, 1966·Proceedings of the Society for Experimental Biology and Medicine·G F LanchantinD W Hart
Jun 1, 1972·Clinica Chimica Acta; International Journal of Clinical Chemistry·R W Colman, B Mitchell
Jul 1, 1965·Biochemical Pharmacology·M E Webster, J P Gilmore
Aug 1, 1972·Annals of Internal Medicine·P WongB M Babior
Sep 1, 1965·Immunochemistry·G ManciniJ F Heremans


Aug 1, 1976·Archives of Biochemistry and Biophysics·B LahiriR W Colman
May 1, 1981·Journal of the Neurological Sciences·L H DickermanR G Macbride
Jan 1, 1986·Critical Reviews in Oncology/hematology·R W Colman, A H Schmaier
May 5, 1983·The New England Journal of Medicine·M SchapiraR W Colman
Oct 1, 1979·European Journal of Biochemistry·C F ScottR W Colman
Jul 1, 1977·The Journal of Clinical Investigation·C Y LiuR W Colman
Feb 1, 1978·The Journal of Clinical Investigation·R W ColmanR H Gilman
Feb 1, 1980·The Journal of Clinical Investigation·C F Scott, R W Colman
Jul 1, 1986·The Journal of Clinical Investigation·E J GustafsonA H Schmaier
Jul 1, 1974·Microvascular Research·A P Kaplan
Mar 1, 1978·Thrombosis Research·M J GallimoreH Stormorken
Apr 1, 1979·Circulation Research·N G Levinsky
Jan 1, 1980·Scandinavian Journal of Clinical and Laboratory Investigation·M Epstein
Nov 6, 2004·The Biochemical Journal·Christina LigoudistianouJohn E Volanakis
Aug 26, 1998·The Journal of Peptide Research : Official Journal of the American Peptide Society·G S GarrettJ M McIver

Related Concepts

Antibody Specificity
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