Cechová D, Jonáková V, Havranová M, Sedláková E, Mach O
Hoppe Seylers Z Physiol Chem. 1979 Dec;360(12):1759-66. doi: 10.1515/bchm2.1979.360.2.1759.
Three natural proteinase isoinhibitors with low isoelectric points BUSI 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 Bl and B2 have identical amino acid composition. Isoinhibitor A contains six amino acid residues less than isoinhibitors B1 and B2. Since sugars have been 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 and chymotrypsin. Glandular kallikrein is also inhibited, but to a very low extent only. The molecular weight (Mr approximately 8 900) was determined by gel filtration.
通过在Sephadex G - 50上进行凝胶过滤以及在DEAE - Sephadex和SE - Sephadex上进行离子交换色谱法,从公牛精浆中分离出三种等电点较低的天然蛋白酶抑制因子,即BUSI I A(pI = 3.9)、BUSI I B1(pI = 3.4)和BUSI I B2(pI = 3.7)。抑制因子B1和B2具有相同的氨基酸组成。抑制因子A比抑制因子B1和B2少六个氨基酸残基。由于在抑制因子中检测到了糖类,其异质性也可能归因于糖成分。这些抑制因子具有相同的抑制特性;它们都能抑制顶体蛋白酶、胰蛋白酶和糜蛋白酶。腺激肽释放酶也受到抑制,但程度非常低。通过凝胶过滤法测定了其分子量(Mr约为8900)。