The role of C1 esterase inhibitor in the activation of C1r, a subcomponent of the first component of complement from human plasma.
Clr was isolated from human serum by DEAE-cellulose column chromatography in the presence of EDTA. The isolated Clr did not hydrolyze N(alpha)-acetyl-L-arginine methyl ester, unless activated by brief treatment with trypsin [EC 3.4.21.4]. On thecolumn, the C1 esterase inhibitor activity was found to coincide with Clr but not C1s (another subcomponent of the first component)  C1r was isolated from the euglobulin fraction of human serum by DEAE-cellulose column chromatograph. On Sephadex G-200 column chromatography, Clr was eluted in the void volume, whereas Clr was eluted in a position corresponding to a molecular weight of 140,000-160,000. The results indicated that, on activation, Clr was converted to an enzyme of lower molecular weight...
D002852:Chromatography, Ion Exchange; D003172:Complement C1 / Q000502:physiology*; D004950:Esterases / Q000037:antagonists & inhibitors*; D006801:Humans; D008970:Molecular Weight; D012712:Serum Globulins; D014357:Trypsin
D003172:Complement C1; D012712:Serum Globulins; D004950:Esterases; D014357:Trypsin