Bellon G, Ooyama T, Hornebeck W, Robert L
Artery. 1980;7(4):290-302.
A serine protease active on insoluble elastin at neutral pH has been isolated from human aortic media employing a Lima-bean trypsin inhibitor - Sepharose column. It is also hydrolyzed Suc (Ala)3 pna and casein but was found inactive against Benzoyl-Tyr-pna and Benzoyl-Arg-pna. Its apparent molecular weight as determined by SDS-PAGE was 22,300 Daltons. It differs from other elastases of human origin (human pancreatic elastase-1, human pancreatic elastase-2, human leucocyte elastase) on the basis of amino-acid composition and immunological specificity.
利用利马豆胰蛋白酶抑制剂-琼脂糖柱从人主动脉中膜分离出一种在中性pH下对不溶性弹性蛋白有活性的丝氨酸蛋白酶。它还能水解Suc（Ala）3 pna和酪蛋白，但对苯甲酰-Tyr-pna和苯甲酰-Arg-pna无活性。通过SDS-PAGE测定其表观分子量为22,300道尔顿。基于氨基酸组成和免疫特异性，它与其他来源的人弹性蛋白酶（人胰腺弹性蛋白酶-1、人胰腺弹性蛋白酶-2、人白细胞弹性蛋白酶）不同。
