荧光假单胞菌对羟基苯甲酸羟化酶的三种最小的溴化氰肽的氨基酸序列。
The amino-acid sequence of the three smallest CNBr peptides from p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.
作者信息
Vereijken J M, Hofsteenge J, Bak H J, Beintema J J
出版信息
Eur J Biochem. 1980 Dec;113(1):151-7. doi: 10.1111/j.1432-1033.1980.tb06149.x.
Abstract
After CNBr cleavage of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens, five peptides and free homoserine were isolated (see preceding paper in this journal). The amino acid sequences of the three smallest peptides, viz. CB3, CB4 and CB5, were determined by automated Edman degradation and analysis of enzymatic subdigests. These peptides form a continuous stretch of 110 residues from the N terminus: (Formula: See Text).
摘要
用溴化氰裂解荧光假单胞菌的对羟基苯甲酸羟化酶后，分离出了五个肽段和游离的高丝氨酸（见本期刊的上一篇论文）。通过自动埃德曼降解法和酶促亚消化分析，确定了三个最小肽段即CB3、CB4和CB5的氨基酸序列。这些肽段从N端开始形成了一段连续的110个残基：（分子式：见正文）。
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