PARTIAL-PURIFICATION OF PHOSPHORAMIDON-SENSITIVE ENDOTHELIN CONVERTING ENZYME IN PORCINE AORTIC ENDOTHELIAL-CELLS - HIGH-AFFINITY FOR RICINUS-COMMUNIS AGGLUTININ

被引：18

作者：

OHNAKA, K ^{[1
]}

NISHIKAWA, M ^{[1
]}

TAKAYANAGI, R ^{[1
]}

HAJI, M ^{[1
]}

NAWATA, H ^{[1
]}

机构：

[1] FUJISAWA PHARMACEUT CO LTD,EXPLORATORY RES LABS,TSUKUBA,IBARAKI 30026,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 185卷 / 02期

关键词：

D O I：

10.1016/0006-291X(92)91668-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：

A membrane-bound endothelin converting enzyme (ECE) of porcine aortic endothelial cells (ECs) was solubilized with Lubrol PX with high efficiency and stability. The solubilized ECE was bound to Ricinus communis agglutinin (RCA) but not to peanut agglutinin (PNA) or wheat germ agglutinin (WGA), suggesting that the ECE has a galactosylated structure possessing a high affinity for RCA. The sequential chromatography on RCA-agarose, PNA-agarose and a TSKgel DEAE-5PW column attained 2,100-fold purification for the ECE over the membrane fractions. The purified ECE was sensitively inhibited by phosphoramidon but not by thiorphan. The present RCA and PNA affinity column procedures may be a powerful approach to isolation of ECE of EC origin. © 1992.

引用

页码：611 / 616

页数：6

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