PURIFICATION AND PARTIAL SEQUENCE-ANALYSIS OF THE SOLUBLE CATECHOL-O-METHYLTRANSFERASE FROM HUMAN PLACENTA - COMPARISON TO THE RAT-LIVER ENZYME

被引：20

作者：

TILGMANN, C

KALKKINEN, N

机构：

[1] UNIV HELSINKI,INST BIOTECHNOL,KARVAAMOKUJA 3,SF-00380 HELSINKI,FINLAND

[2] ORION CORP,MOLEC GENET LAB,SF-00380 HELSINKI,FINLAND

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 174卷 / 02期

关键词：

D O I：

10.1016/0006-291X(91)91517-G

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：

Catechol-o-methyltransferase from human placenta was purified 1400-fold by hydroxyapatite adsorption, ammonium sulfate precipitation, gel filtration, high performance anion- exchange and reversed-phase chromatography. The purified enzyme has an apparent molecular weight of 26.000, an isoelectric point of 5,3 and is activated ten-fold in the presence of 20mM cysteine. The enzyme shows primary structure homology to the corresponding rat liver soluble enzyme, based on the sequenced tryptic peptides. © 1991.

引用

页码：995 / 1002

页数：8

共 29 条

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