Basophil kallikrein of anaphylaxis (BK-A)--purification and characterization.
These studies describe the IgE-mediated release of a basophil kallikrein of anaphylaxis (BK-A) that has arginine esterase activity and is inhibited by plasma, DFP, and Trasylol. The interaction of BK-A active fractions from ion exchange (DEAE-Sephacel) and gel filtration (Sepharose 6B) chromatography, with human plasma kininogen generates immunoreactive kinin. The BK-A and kinin-generating activities co-chromatograph on DEAE-Sephacel and Sepharose 6B columns, and the quantity of kinin generated is, in general, proportional to the BK-A activity of the column fractions, suggesting that these two activities are subserved by the same protease. These data suggest that kallikrein-like activity can be generated from human basophils as a direct result of a primary IgE-mediated immune reaction, thus providing a potential link between reactions of immediate hypersensitivity and the plasma and/or tissue kinin-generating systems.
D000707:Anaphylaxis / Q000503:physiopathology*; D001120:Arginine; D001491:Basophils / Q000502:physiology*; D006801:Humans; D007073:Immunoglobulin E; D007610:Kallikreins / Q000097:blood* / Q000276:immunology / Q000302:isolation & purification; D007700:Kinetics; D007705:Kinins / Q000378:metabolism; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000097:blood / Q000302:isolation & purification; D013379:Substrate Specificity
D007705:Kinins; D007073:Immunoglobulin E; D001120:Arginine; D010447:Peptide Hydrolases; D007610:Kallikreins