Pivnenko T N, Epshteĭn L M, Okladnikova S V, Gazha A K, Besednova N N
Pacific Fishery Research Center, Vladivostok, Russia.
Prikl Biokhim Mikrobiol. 1998 Jul-Aug;34(4):455-9.
Peptides with molecular weights of 0.8 to 16 kDa were isolated from the keratinous envelope of chicken muscular stomach cuticle. The peptide preparation had a immunostimulating activity whose qualitative and quantitative traits made it comparable with the activity of known drugs of similar composition. In addition, the peptide preparation reversibly inactivated trypsin and activated chymotrypsin. A low-molecular-weight protein (14.1 kDa) was isolated from the peptide preparation by affinity chromatography on trypsin-Sepharose 4B. This protein was found to be a reversible noncompetitive inhibitor of trypsin.
从鸡肌胃角质膜中分离出分子量为0.8至16 kDa的肽。该肽制剂具有免疫刺激活性,其定性和定量特征使其与已知的类似组成药物的活性相当。此外,该肽制剂可使胰蛋白酶可逆失活并激活糜蛋白酶。通过在胰蛋白酶-琼脂糖4B上进行亲和层析,从该肽制剂中分离出一种低分子量蛋白质(14.1 kDa)。发现该蛋白质是胰蛋白酶的可逆非竞争性抑制剂。