Schmidt M, Kröger B, Jacob E, Seulberger H, Subkowski T, Otter R, Meyer T, Schmalzing G, Hillen H
Department of Pharmaceutical Research, BASF Aktiengesellschaft, Ludwigshafen, Germany.
FEBS Lett. 1994 Dec 19;356(2-3):238-43. doi: 10.1016/0014-5793(94)01277-6.
A membrane-bound protease activity that specifically converts Big endothelin-1 has been purified from bovine endothelial cells (FBHE). The enzyme was cleaved with trypsin and the peptide sequencing analysis confirmed it to be a zinc chelating metalloprotease containing the typical HEXXH (HELTH) motif. RT-PCR and cDNA screens were employed to isolate the complete cDNAs of the bovine and human enzymes. This human metalloprotease was expressed heterologously in cell culture and oocytes. The catalytic activity of the recombinant enzyme is the same as that determined for the natural enzyme. The data suggest that the characterized enzyme represents the functional human endothelin converting enzyme ECE-1.
一种能特异性转化大内皮素-1的膜结合蛋白酶活性已从牛内皮细胞（FBHE）中纯化出来。该酶用胰蛋白酶切割，肽序列分析证实它是一种含有典型HEXXH（HELTH）基序的锌螯合金属蛋白酶。采用RT-PCR和cDNA筛选来分离牛和人酶的完整cDNA。这种人金属蛋白酶在细胞培养和卵母细胞中进行了异源表达。重组酶的催化活性与天然酶所测定的活性相同。数据表明，所鉴定的酶代表功能性人内皮素转化酶ECE-1。
