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- W980091489 abstract "Studies on a trypsin inhibitor in guinea pig seminal vesicles were initiated by Haendle et al. Furthermore investigation of inhibitor preparations obtained by affinity chromatography on trypsin resin revealed the presence of two inhibitors, distinguishable on the basis of inhibition characteristics and physical and chemical properties: the one was characterized as a trypsin inhibitor, TI; the other as a trypsin-plasmin inhibitor, TPI. Their physiological role was unknown. In 1968 Stambaugh and Buckley described a proteinase localized in the acrosome of mammalian spermatozoa, which is responsible for penetration of the sperm through the zona pellucida of the egg. Following the suggestion of Zaneveld, this enzyme was named acrosin. Both inhibitors from guinea pig seminal vesicles turned out to be potent inhibitors of acrosins from various species. This finding, which suggested an important function of proteinase inhibitors in fertilization, stimulated investigations of trypsin inhibitors from the male reproductive system of other species. This chapter examines the assay principle: Both trypsin and plasmin hydrolyze Nα-benzoyl-DL-arginine p-nitroanilide (DL-BAPA). The enzyme activity is measured by following the change in absorbance at 405 nm. Inhibitory activity is measured by the reduction of enzymic activity. It also details the isolation methods and properties of the proteinase inhibitors." @default.
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- W980091489 date "1976-01-01" @default.
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- W980091489 title "[73] Proteinase nhibitors from guinea pig seminal vesicles" @default.
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- W980091489 doi "https://doi.org/10.1016/s0076-6879(76)45076-0" @default.
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