Toyohara H, Makinodan Y, Ikeda S
Comp Biochem Physiol B. 1985;80(4):949-54. doi: 10.1016/0305-0491(85)90489-4.
A trypsin inhibitor was purified from carp muscle to apparent homogeneity by the successive chromatographies of DEAE-cellulose, DEAE-Sepharose CL-6B, Con A-Sepharose, Ultrogel AcA 44 and hydroxylapatite. The mol. wt of the inhibitor was estimated to be 58,000 by SDS-polyacrylamide gel electrophoresis or 50,000 by gel filtration. The inhibitor seemed to form a 1:1 stoichiometric complex with trypsin, alpha-chymotrypsin and elastase, respectively. Carp muscle trypsin inhibitor was likely to be identical with serum alpha 1-proteinase inhibitor judging from its glycoprotein nature, mol. wt and the inhibition stoichiometry.
通过DEAE - 纤维素、DEAE - 琼脂糖CL - 6B、伴刀豆球蛋白A - 琼脂糖、Ultrogel AcA 44和羟基磷灰石的连续层析，从鲤鱼肌肉中纯化出一种胰蛋白酶抑制剂，达到表观均一性。通过SDS - 聚丙烯酰胺凝胶电泳估计该抑制剂的分子量为58,000，通过凝胶过滤法估计为50,000。该抑制剂似乎分别与胰蛋白酶、α - 胰凝乳蛋白酶和弹性蛋白酶形成1:1化学计量比的复合物。从鲤鱼肌肉胰蛋白酶抑制剂的糖蛋白性质、分子量和抑制化学计量比判断，它可能与血清α1 - 蛋白酶抑制剂相同。
