Partial purification of phosphoramidon-sensitive endothelin converting enzyme in porcine aortic endothelial cells: High affinity for Ricinus communis agglutinin

Keizo Ohnaka, Motoaki Nishikawa, Ryoichi Takayanagi, Masafumi Haji, Hajime Nawata

研究成果: Contribution to journalArticle査読

14 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)611-616
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
185
2
DOI
出版ステータス出版済み - 6 15 1992

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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