大鼠肝脏组织蛋白酶L对胰高血糖素的作用。
Action of rat liver cathepsin L on glucagon.
作者信息
Kärgel H J, Dettmer R, Etzold G, Kirschke H, Bohley P, Langner J
出版信息
Acta Biol Med Ger. 1981;40(9):1139-43.
PMID:7340337
Abstract
The proteolytic specificity of cathepsin L on glucagon was determined. Major cleavages are found between Thr7 and Ser8, Asp15 and Ser16, and between Met27 and Asn28. The bonds Ser11-Lys12, Val23-Gln24, and Gln24-Trp25 are hydrolyzed to a relatively low extent only. Whereas cathepsin B hydroxyzes glucagon at the C-terminus by a peptidyldipeptidase mechanism, cathepsin L cleaves the same substrate clearly as endopeptidase.
摘要
测定了组织蛋白酶L对胰高血糖素的蛋白水解特异性。主要裂解发生在苏氨酸7和丝氨酸8之间、天冬氨酸15和丝氨酸16之间以及甲硫氨酸27和天冬酰胺28之间。丝氨酸11-赖氨酸12、缬氨酸23-谷氨酰胺24和谷氨酰胺24-色氨酸25之间的肽键仅在相对较低程度上被水解。组织蛋白酶B通过肽基二肽酶机制在C端水解胰高血糖素，而组织蛋白酶L则明显以内肽酶的方式裂解相同的底物。
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