Vered M, Gertler A, Burstein Y
Int J Pept Protein Res. 1986 Feb;27(2):183-90. doi: 10.1111/j.1399-3011.1986.tb01809.x.
The partial amino acid sequence of porcine elastase II, isolated from crude trypsin Type II, was determined. The enzyme consists of two polypeptide chains, a light chain composed of 11 residues, and a heavy chain (Mr = 23 500) with four intrachain disulfide bridges; the two chains are held together by one interchain disulfide bond. Elastase II was fragmented into several peptides by chemical cleavages with CNBr at the two methionine residues, 99 and 180 (chymotrypsinogen numbering), and with hydroxylamine at the peptide bond following DIP-Ser195. About 50% of the sequence was determined and the positions of 120 amino acids were located, including the light chain residues and most of the active site residues. The partial sequence shows 64% difference between porcine elastase II and elastase I and only 26% difference between porcine elastase II and bovine chymotrypsin B.
测定了从粗制II型胰蛋白酶中分离得到的猪弹性蛋白酶II的部分氨基酸序列。该酶由两条多肽链组成，一条轻链由11个残基组成，一条重链（Mr = 23500）有四个链内二硫键；两条链通过一个链间二硫键连接在一起。弹性蛋白酶II通过在两个甲硫氨酸残基（99和180，按照胰凝乳蛋白酶原编号）处用CNBr进行化学裂解，以及在DIP-Ser195之后的肽键处用羟胺进行化学裂解，被切割成几个肽段。测定了约50%的序列，并确定了120个氨基酸的位置，包括轻链残基和大部分活性位点残基。部分序列显示猪弹性蛋白酶II与弹性蛋白酶I之间有64%的差异，而猪弹性蛋白酶II与牛胰凝乳蛋白酶B之间只有26%的差异。
