Basophil kallikrein of anaphylaxis (BK-A)--purification and characterization.

Abstract

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.

• Authors: H H Newball, R W Berninger, R C Talamo, L M Lichtenstein
• Journal: Advances in experimental medicine and biology (Adv Exp Med Biol) Vol. 120B Pg. 233-47 ( 1979) ISSN: 0065-2598 [Print] United States
• PMID: 517236 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Kinins
• Immunoglobulin E
• Arginine
• Peptide Hydrolases
• Kallikreins

Topics

• Anaphylaxis (physiopathology)
• Arginine
• Basophils (physiology)
• Humans
• Immunoglobulin E
• Kallikreins (blood, immunology, isolation & purification)
• Kinetics
• Kinins (metabolism)
• Molecular Weight
• Peptide Hydrolases (blood, isolation & purification)
• Substrate Specificity