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Determination of intermediates, products and cleavage site in the reaction between plasminogen activator inhibitor type‐2 and urokinases
Author(s) -
Kiso U.,
Kaudewitz H.,
Henschen A.,
Åstedt B.,
Kruithof E.K.O.,
Bachmann F.
Publication year - 1988
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(88)80640-9
Subject(s) - cleavage (geology) , chemistry , plasminogen activator , stereochemistry , biochemistry , combinatorial chemistry , biology , endocrinology , paleontology , fracture (geology)
Several specific inhibitors for plasminogen activators have been isolated from various organs and cell lines, those from human placenta and the human monocyte‐like cell line U‐937 being virtually identical. The reaction between this type of inhibitor, designated as type‐2, and high‐ M r and low‐ M r urokinase‐type plasminogen activators was followed by reversed‐phase high‐performance liquid chromatography and gel electrophoresis. The components, their stable complexes and their dissociation and cleavage products could be clearly identified in both systems. The amino acid sequence of the inhibitor at the cleavage site was determined to be ‐Met‐Thr‐Gly‐Arg↓Thr‐Gly‐His‐Gly‐. A 35‐residue carboxy‐terminal fragment was found to be released.