REMOVAL OF COVALENTLY BOUND INOSITOL FROM TORPEDO ACETYLCHOLINESTERASE AND MAMMALIAN ALKALINE-PHOSPHATASES BY DEAMINATION WITH NITROUS-ACID - EVIDENCE FOR A COMMON MEMBRANE-ANCHORING STRUCTURE

被引：65

作者：

LOW, MG

FUTERMAN, AH

ACKERMANN, KE

SHERMAN, WR

SILMAN, I

机构：

[1] WEIZMANN INST SCI,DEPT NEUROBIOL,IL-76100 REHOVOT,ISRAEL

[2] WASHINGTON UNIV,SCH MED,DEPT PSYCHIAT,ST LOUIS,MO 63110

来源：

BIOCHEMICAL JOURNAL | 1987年 / 241卷 / 02期

关键词：

D O I：

10.1042/bj2410615

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：

引用

页码：615 / 619

页数：5

共 21 条

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[6] IDENTIFICATION OF COVALENTLY BOUND INOSITOL IN THE HYDROPHOBIC MEMBRANE-ANCHORING DOMAIN OF TORPEDO ACETYLCHOLINESTERASE [J].

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[10] COVALENTLY ATTACHED PHOSPHATIDYLINOSITOL AS A HYDROPHOBIC ANCHOR FOR MEMBRANE-PROTEINS [J].

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