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Inactivation of human plasma α 1 ‐proteinase inhibitor by human PMN leucocyte collagenase
Author(s) -
Knäuper Vera,
Reinke Heinz,
Tschesche Harald
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81412-h
Subject(s) - collagenase , incubation , proteinase inhibitor , chemistry , human plasma , enzyme inhibitor , cleavage (geology) , high performance liquid chromatography , microbiology and biotechnology , biochemistry , enzyme , chromatography , biology , paleontology , fracture (geology)
Highly purified human polymorphonuelear leucocyte collagenase cleaved human α‐1‐proteinase inhibitor (α 1 ‐PI) at the carboxyl site of Phe 352 (P 7 ). 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 Pro 357 (P 2 ).