通过自溶作用溶解的猪肾二肽基肽酶IV的N端氨基酸序列。
N-terminal amino-acid sequence of pig kidney dipeptidyl peptidase IV solubilized by autolysis.
作者信息
Seidl R, Mann K, Schäfer W
机构信息
Max-Planck-Institut für Biochemie, Martinsried bei München.
出版信息
Biol Chem Hoppe Seyler. 1991 Mar;372(3):213-4. doi: 10.1515/bchm3.1991.372.1.213.
PMID:1675855
Abstract
The N-terminal amino-acid sequence of the intrinsic membrane protein dipeptidyl peptidase IV (DP IV) was determined. The protein was isolated from pig kidney and solubilized by autolysis at pH 3.8. The first 34 amino acids were sequenced and indicated approximately 78% identity to the N-terminal sequence of rat liver DP IV.
摘要
测定了内在膜蛋白二肽基肽酶IV（DP IV）的N端氨基酸序列。该蛋白从猪肾中分离出来，并在pH 3.8下通过自溶作用溶解。测定了前34个氨基酸的序列，结果表明其与大鼠肝脏DP IV的N端序列约有78%的同源性。
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