来自中华猕猴桃果实中的蛋白水解酶——猕猴桃蛋白酶的胰蛋白酶肽段的氨基酸序列。
The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis.
作者信息
Carne A, Moore C H
出版信息
Biochem J. 1978 Jul 1;173(1):73-83. doi: 10.1042/bj1730073.
Abstract
The amino acid sequences of the tryptic peptides of the thiol proteinase actinidin from Actinidia chinensis were determined by the manual dansyl--Edman procedure. There are 12 tryptic peptides, which give a polypeptide chain of 220 residues with a mol.wt. of 23500. An alignment of the tryptic peptides was made by using the X-ray-crystallographic data of Baker [(1977) J. Mol. Biol. 115, 263--277] determined at 0.28 nm resolution on crystalline actinidin. Detailed evidence for the amino acid sequences of the tryptic peptides has been deposited as Supplementary Publication SUP 50083 (14 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.
摘要
采用手工丹磺酰 - 埃德曼法测定了中华猕猴桃中硫醇蛋白酶肌动蛋白水解酶胰蛋白酶肽段的氨基酸序列。有12个胰蛋白酶肽段，它们构成了一条含有220个残基、分子量为23500的多肽链。利用贝克[（1977年）《分子生物学杂志》115卷，263 - 277页]在0.28纳米分辨率下测定的结晶肌动蛋白水解酶的X射线晶体学数据，对胰蛋白酶肽段进行了比对。胰蛋白酶肽段氨基酸序列的详细证据已作为补充出版物SUP 50083（共14页）存放在英国西约克郡韦瑟比波士顿温泉市英国国家图书馆文献供应中心，邮编LS23 7BQ，可按《生物化学杂志》（1978年）169卷第5页所示条件从该处获取复印件。
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