Identification of endothelin converting enzyme in bovine lung membranes using a new fluorogenic substrate.
Identification of endothelin converting enzyme in bovine lung membranes using a new fluorogenic substrate.
复制标题
使用新的荧光底物鉴定牛肺膜中的内皮素转换酶。
DOI：
10.1016/0024-3205(92)90175-o
复制
发表时间：
1992
期刊：
影响因子：
6.1
通讯作者：
Wilson,IB
中科院分区：
文献类型：
--
作者：
Kundu,GC;Wilson,IB
An enzyme partially purified from bovine lung membranes appears to be endothelin converting enzyme (ECE). This enzyme specifically cleaves big endothelin-1 (big ET-1) at the proper site, between Trp21and Va122, with maximum activity at pH 7.5 and with a Kmof roughly 3 μM, to produce endothelin-1 (ET-1) and C-terminal peptide (CTP). This same enzyme hydrolyzes the fluorogenic substrate succinyl-Ile-Ile-Trp-methylcoumarinamide to release the highly fluorescent 7-amino-4-methylcoumarin. The peptide derivative has the same amino acid sequence as big ET-1 and is a good substrate with a Kmof about 27 μM. This enzyme is a metalloproteinase. It is not inhibited by five common proteinase inhibitors (pepstatin A, PMSF, NEM, E-64 and thiorphan) but it is inhibited by phosphoramidon and chelating compounds. The apoenzyme is restored to nearly full activity by a zinc-EDTA buffer with pZn = 13.
