Ward C W
Biochim Biophys Acta. 1975 May 23;391(1):201-11. doi: 10.1016/0005-2744(75)90167-9.
The major form of the trypsin-like proteinases from the larvae of the webbing clothes moth Tineola bisselliella has been further purified and some of its properties investigated. It differs from bovine trypsin in several respects. It is anionic at neutral pH, is very stable at alkaline pH, has no requirement for calcium ions for this stability and is very sensitive to urea. It resembles vertebrate trypsins in its complete inhibition by diisopropylfluorophosphate, its pH optimum of 8.5 for hydrolysis of benzoyl-arginine p-nitroanilide and its cleavage specificity against glucagon and the beta-chain of S-carboxymethyl insulin.
织网衣蛾谷蛾幼虫体内类胰蛋白酶的主要形式已得到进一步纯化，并对其一些特性进行了研究。它在几个方面与牛胰蛋白酶不同。在中性pH值下它呈阴离子状态，在碱性pH值下非常稳定，这种稳定性不需要钙离子，并且对尿素非常敏感。在被二异丙基氟磷酸完全抑制、水解对硝基苯甲酰精氨酸时的最适pH值为8.5以及对胰高血糖素和S-羧甲基胰岛素β链的切割特异性方面，它与脊椎动物的胰蛋白酶相似。
