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PURIFICATION AND CHARACTERIZATION OF PUTATIVE ENDOTHELIN CONVERTING ENZYME IN BOVINE ADRENAL-MEDULLA - EVIDENCE FOR A CATHEPSIN D-LIKE ENZYME

被引：89
作者：
SAWAMURA, T
KIMURA, S
SHINMI, O
SUGITA, Y
YANAGISAWA, M
GOTO, K
MASAKI, T
机构：
[1] UNIV TSUKUBA,INST BASIC MED SCI,DEPT BIOCHEM,TSUKUBA,IBARAKI 305,JAPAN
[2] UNIV TSUKUBA,INST BASIC MED SCI,DEPT PHARMACOL,TSUKUBA,IBARAKI 305,JAPAN
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 168卷 / 03期
关键词：
D O I：
10.1016/0006-291X(90)91160-T
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 specific and sensitive assay has been established for measurement of endothelin converting activity in a tissue extract. This assay is based on measuring endothelin-1 generated from big endothelin-1 by endothelin converting enzyme (ECE) with radioimmunoassay using an endothelin C-terminal specific antibody. By using this assay, we purified and characterized ECE in bovineadrenomedullary chromaffin granules. ECE was purified over 3,000 times by a combination of DEAE, hydrophobic and gel filtration chromatography. A molecular weight of ECE was estimated to be approximately 30,000 by gel filtration. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that ECE had three major components with estimated molecular weights of 45,000, 30,000 and 15,000 like bovine spleen cathepsin D. ECE had a pH optimum at 3.5 and was inhibited by pepstatin. These results strongly suggest that ECE is a cathepsin D-like aspartic protease. © 1990.
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页码：1230 / 1236
页数：7
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