Abstract
Abstract
Trypsin inhibitors isolated from human urine and highly purified by affinity chromatography displayed molecular weights of 43,000 (H-UTI) and 22,000 (L-UTI) during sodium dodecyl sulfate-polyacrylamide gel electrophoresis. These molecules not only inhibited trypsin [EC 3.4.21.4], chymotrypsin [EC 3.4.21.1], and plasmin [EC 3.4.21.7], but also showed strong inhibitory effects on the human sperm enzyme, acrosin [EC 3.4.21.10]. A novel protease inhibitor (anticin) which specifically reacted with SH-proteases, such as ficin [EC 3.4.22.3], papain [EC 3.4.22.2], and bromelain [EC 3.4.22.4], was also isolated from normal human urine.
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