CHARACTERIZATION OF PHOSPHOLIPID METHYLATION IN RAT-BRAIN MYELIN

被引：11

作者：

TSVETNITSKY, V ^{[1
]}

AUCHI, L ^{[1
]}

NICOLAOU, A ^{[1
]}

GIBBONS, WA ^{[1
]}

机构：

[1] UNIV LONDON,IND CTR PHARMACEUT RES,SCH PHARM,LONDON WC1N 1AX,ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1995年 / 307卷

关键词：

D O I：

10.1042/bj3070239

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：

Highly purified rat brain myelin was solubilized in Triton X-100 and myelin phospholipid N-methyltransferase was characterized. The enzyme activities were separated by isoelectric focusing and ion-exchange chromatography. The phospholipid methyltransferase has shown at least four peaks of activity with pI(app). values of 4.5, 5.2, 6.2 and 8.4. After affinity purification each of these activities revealed a close set of bands of approx. 65 kDa on SDS/PAGE. These data together with those from preparative SDS/PAGE separations suggested that rat brain myelin contains three acidic and at least one basic phospholipid-methylating isoenzymes and that the major isoenzyme in each case is approx. 65 kDa in size. While the predominant product of the reaction catalysed by all detected isoforms was monomethylated phosphatidylethanolamine, the least acidic isoform (pI(app.) 6.2) also formed about 20% phosphatidylcholine, suggesting that these isoenzymes may play different roles in vivo.

引用

页码：239 / 244

页数：6

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