Amino acid sequence of bovine white matter proteolipid.

Amino acid sequence of bovine white matter proteolipid.
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牛白质蛋白脂质的氨基酸序列。

DOI:
10.1016/0003-9861(83)90334-x
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发表时间:
1983
影响因子:
3.9
通讯作者:
Laursen,RA
Laursen,RA
中科院分区:
生物学3区
文献类型:
--
作者:
Lees,MB;Chao,BH;Lin,LF;Samiullah,M;Laursen,RA

文献摘要

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通过蛋白质分解和色氨酸残基的化学裂解相结合的方法研究了牛白质蛋白脂的序列。经胰酶、胰凝乳酶、梭状芽孢杆菌酶和金黄色葡萄球菌蛋白酶消化得到的多肽序列由氨基末端的52个残基、羧基末端的96个残基和几个附加片段组成。用2-(2-nitrophenylsulfenyl)-3-methyl-3′-bromoindolenine处理该蛋白获得的多肽证实了序列的比对并延长了序列。这些信息,结合其他研究人员的信息,使我们能够提出整个蛋白质的一级结构。在序列测定的基础上,该蛋白脂蛋白的相对分子质量为29,869。
The sequence of the bovine white matter proteolipid has been studied by a combination of proteolytic digestion and chemical cleavage at tryptophan residues. Alignment of peptides obtained by digestion with trypsin, chymotrypsin, clostripain, andStaphylococcus aureusprotease gave the sequence of 52 residues at the amino terminus, 96 residues at the carboxyl terminus, and several additional segments. Peptides obtained by treatment of the protein with 2-(2-nitrophenylsulfenyl)-3-methyl-3′-bromoindolenine confirmed the alignment and extended the sequence. This information, combined with that of other investigators, permits us to propose the primary structure for the entire protein. On the basis of the sequence determination, the molecular weight of the proteolipid protein is 29,869.