牛刷状缘膜囊泡中肾氨肽酶N的寡聚结构。
The oligomeric structure of renal aminopeptidase N from bovine brush-border membrane vesicles.
作者信息
Plakidou-Dymock S, McGivan J D
机构信息
Department of Biochemistry, School of Medical Sciences, Bristol, UK.
出版信息
Biochim Biophys Acta. 1993 Jan 18;1145(1):105-12. doi: 10.1016/0005-2736(93)90386-e.
Abstract
Bovine renal brush-border membrane vesicle aminopeptidase N at various stages of purity was treated with two bifunctional cross-linking agents. A pattern of emergence of higher molecular weight forms was observed. By using a cleavable cross-linker, aminopeptidase N was shown to cross-link both to itself and to its breakdown products as well as to dipeptidyl peptidase IV. Using this technique it was possible to identify three of the breakdown products as 45 kDa, 66 kDa and 95 kDa peptides. N-terminal amino acid sequence analysis was used to define the precise cleavage points for the bovine renal aminopeptidase N breakdown products. The short amino acid sequences obtained show strong sequence similarity with the human intestinal and rat kidney aminopeptidase N.
摘要
用两种双功能交联剂处理处于不同纯度阶段的牛肾刷状缘膜囊泡氨肽酶N。观察到出现了更高分子量形式的模式。通过使用可裂解交联剂，显示氨肽酶N既能自身交联，也能与其降解产物以及二肽基肽酶IV交联。利用该技术能够鉴定出三种降解产物为45 kDa、66 kDa和95 kDa的肽。N端氨基酸序列分析用于确定牛肾氨肽酶N降解产物的精确切割点。所获得的短氨基酸序列与人肠道和大鼠肾脏氨肽酶N具有很强的序列相似性。
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