HUMAN-MILK BILE-SALT STIMULATED LIPASE - SEQUENCE SIMILARITY WITH RAT LYSOPHOSPHOLIPASE AND HOMOLOGY WITH THE ACTIVE-SITE REGION OF CHOLINESTERASES

被引：17

作者：

CHRISTIE, DL ^{[1
]}

CLEVERLY, DR ^{[1
]}

OCONNOR, CJ ^{[1
]}

机构：

[1] UNIV AUCKLAND,DEPT CHEM,AUCKLAND,NEW ZEALAND

来源：

FEBS LETTERS | 1991年 / 278卷 / 02期

关键词：

HUMAN MILK BILE-SALT STIMULATED LIPASE; LYSOPHOSPHOLIPASE; ACTIVE SITE; ACETYLCHOLINESTERASE;

D O I：

10.1016/0014-5793(91)80114-I

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

To determine the active site residue, human milk bile-salt stimulated lipase (BSSL) was labelled with [H-3]diisopropyl fluorophosphate (DFP). Partial sequence analysis of cyanogen bromide fragments (a total of 146 residues from 6 peptides) revealed 84% sequence identity with a putative rat lysophospholipase. Sequence analysis of a [H-3]DFP-labelled peptide indicated that the active site serine was contained in the sequence Gly-Glu-Ser-Ala-Gly. In addition to similarity with rat lysophospholipase, this sequence showed homology with regions of human butyrylcholinesterase and electric ray acetylcholinesterase (68% identity). It is concluded that these proteins are members of a new supergene family.

引用

页码：190 / 194

页数：5

共 19 条

[1] HUMAN-MILK BILE-SALT STIMULATED LIPASE - FURTHER INVESTIGATIONS ON THE AMINO-ACIDS RESIDUES INVOLVED IN THE CATALYTIC SITE [J].