Sinha S, Watorek W, Karr S, Giles J, Bode W, Travis J
Proc Natl Acad Sci U S A. 1987 Apr;84(8):2228-32. doi: 10.1073/pnas.84.8.2228.
The complete amino acid sequence of human neutrophil elastase has been determined. The protein consists of 218 amino acid residues, contains two asparagine-linked carbohydrate side chains, and is joined together by four disulfide bonds. Comparison of the sequence to other serine proteinases indicates only moderate homology with porcine pancreatic elastase (43.0%) or neutrophil cathepsin G (37.2%). In particular, many of the residues suggested to play important roles in the mechanism by which the pancreatic elastase functions are significantly changed in the neutrophil enzyme, indicating alternative types of binding with the human proteinase.
人中性粒细胞弹性蛋白酶的完整氨基酸序列已被确定。该蛋白质由218个氨基酸残基组成，含有两条天冬酰胺连接的碳水化合物侧链，并通过四个二硫键连接在一起。将该序列与其他丝氨酸蛋白酶进行比较表明，与人胰腺弹性蛋白酶（43.0%）或中性粒细胞组织蛋白酶G（37.2%）只有中等程度的同源性。特别是，许多在胰腺弹性蛋白酶发挥功能的机制中被认为起重要作用的残基，在中性粒细胞酶中发生了显著变化，这表明与人类蛋白酶存在不同类型的结合。
