马微纤溶酶原完整氨基酸序列。

Protein sequences & data analysis Pub Date : 1991-08-01
J Schaller, C Straub, U Kämpfer, E E Rickli
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引用次数: 0

摘要

用2-(2-nitrophenylsulfenyl)-3-methyl-3'- bromoindoline、溴化氰或clostripain裂解得到的片段,测定了马微小纤溶酶原的完整氨基酸序列(Mr为37,132,338个残基)。这些片段按重叠序列排列。与其他物种的序列比较,其同源性分别为76%(牛)和81%(犬),表明其存在与其他物种相同的结构域和功能域。不同微纤溶酶原的序列比较表明,49 (Arg)、83 (Arg)和161 (Ser)位点可能在纤溶酶原与链激酶相互作用中起作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Complete amino acid sequence of equine miniplasminogen.

The complete amino acid sequence of equine miniplasminogen (Mr 37,132, 338 residues) was determined with the aid of fragments obtained by cleavage with 2-(2-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine, cyanogen bromide or clostripain. The fragments were aligned with overlapping sequences. Sequence comparison with other species gave identities in the range of 76% (bovine) and 81% (canine), indicating the presence of the same structural and functional domains as in the other species. Sequence comparison of different miniplasminogens showed that positions 49 (Arg), 83 (Arg) and 161 (Ser) may play a role in the interaction between plasminogen and streptokinase.

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