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

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Abstract

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.

Original languageEnglish
Pages (from-to)611-616
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume185
Issue number2
DOIs
Publication statusPublished - Jun 15 1992

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All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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