Isolation of Acidic Acrosin Isoinhibitors (BUSI I A, BUSI I B1 and BUSI I B2) from Bull Seminal Plasma
- 1 January 1979
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 360 (2) , 1759-1766
- https://doi.org/10.1515/bchm2.1979.360.2.1759
Abstract
Three natural proteinase isoinhibitors with low isoelectric points BUSI [bull seminal plasma inhibitor] I A (pI = 3.9), BUSI I B1 (pI= 3.4) and BUSI I B2 (pI = 3.7) were isolated from bull seminal plasma by gel filtration on Sephadex G-50 and ion exchange chromatography on DEAE-Sephadex and SE-Sephadex. Isoinhibitors B1 and B2 have identical amino acid composition. Isoinhibitor A contains 6 amino acid residues less than isoinhibitors B1 and B2. Since sugars were detected in the isoinhibitors, heterogeneity may also be due to the sugar component. The isoinhibitors show the same inhibitory properties; all of them inhibit acrosin, trypsin (EC 3.4.21.4) and chymotrypsin (EC 3.4.21.1). Glandular kallikrein is also inhibited, but to a very low extent only. The MW (.apprx. 8900) was determined by gel filtration.This publication has 3 references indexed in Scilit:
- Isolation of Basic Acrosin Inhibitor from Bull Seminal Plasma (BUSI II)Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1979
- Aminosäure-p-nitroanilide als Substrate für Aminopeptidasen und andere proteolytische FermenteHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1962
- A spectrophotometric determination of trypsin and chymotrypsinBiochimica et Biophysica Acta, 1955