Inactivation of human plasma alpha 1-proteinase inhibitor by human PMN leucocyte collagenase.
Highly purified human polymorphonuclear leucocyte collagenase cleaved human alpha-1-proteinase inhibitor (alpha 1-PI) at the carboxyl site of Phe352 (P7). The inhibitor was thereby rapidly inactivated and generated a primary degradation product as shown by reverse-phase HPLC and N-terminal sequencing. Prolonged incubation of the modified inhibitor with polymorphonuclear leucocyte collagenase led to the generation of a secondary degradation product with additional cleavage at the carboxyl site of Pro357 (P2).
Knäuper
V
V
University of Bielefeld, Faculty of Chemistry, Department of Biochemistry, FRG.
Reinke
H
H
Tschesche
H
H
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D003012:Microbial Collagenase / Q000097:blood*; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000201:enzymology*; D000515:alpha 1-Antitrypsin / Q000378:metabolism*
D000515:alpha 1-Antitrypsin; D003012:Microbial Collagenase