Production of chemotactic factor for lymphocyte by digestion of IgG with a highly purified polymorphonuclear leukocyte neutral thiol proteinase.
In the present study, we purified a neutral thiol proteinase from dog PMN leukocytes and indicated that the proteinase elaborated the chemotactic factor for lymphocytes by cleavage of IgG. The neutral thiol proteinase was purified about 744-fold by ion-exchange chromatographies and affinity chromatography, and the final preparation was over 70% pure. After incubation of dog IgG with the proteinase, three distinct protein peaks were seen by the gel filtration on Sephadex G-200. Only the third peak, perhaps a dialyzable peptide, showed a significant chemotactic activity for dog lymphocytes.
D000818:Animals; D002630:Chemotactic Factors / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003546:Cysteine Endopeptidases / Q000302:isolation & purification / Q000494:pharmacology*; D015853:Cysteine Proteinase Inhibitors; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007074:Immunoglobulin G / Q000378:metabolism*; D009504:Neutrophils / Q000201:enzymology*
D002630:Chemotactic Factors; D015853:Cysteine Proteinase Inhibitors; D004791:Enzyme Inhibitors; D007074:Immunoglobulin G; D003546:Cysteine Endopeptidases