人组织蛋白酶L的弹性蛋白酶活性
Elastinolytic activity of human cathepsin L.
作者信息
Mason R W, Johnson D A, Barrett A J, Chapman H A
出版信息
Biochem J. 1986 Feb 1;233(3):925-7. doi: 10.1042/bj2330925.
Abstract
The hydrolysis of a tritiated elastin substrate by the human cysteine proteinases cathepsins B and L has been studied. Cathepsin L was found to be at least 100-fold more active on this substrate than cathepsin B. The specific activity of cathepsin L at pH 5.5 for hydrolysis of elastin was about the same as that of pig pancreatic elastase at its optimum pH of 8.8.
摘要
已对人半胱氨酸蛋白酶组织蛋白酶B和L对氚标记弹性蛋白底物的水解作用进行了研究。发现组织蛋白酶L对该底物的活性比组织蛋白酶B至少高100倍。组织蛋白酶L在pH 5.5时水解弹性蛋白的比活性与猪胰弹性蛋白酶在其最适pH 8.8时的比活性大致相同。
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