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人骨髓瘤免疫球蛋白(IgG New)VH区的氨基酸序列。

Amino acid sequence of the VH region of a human myeloma immunoglobulin (IgG New).

作者信息

Poljak R J, Nakashima Y, Chen B L, Konigsberg W

出版信息

Biochemistry. 1977 Jul 26;16(15):3412-20. doi: 10.1021/bi00634a019.

Abstract

The amino acid sequence of the heavy-chain variable region of the human immunoglobulin. New has been determined. Since the amino terminus of the heavy chain was blocked, the sequence of residues 1-69 was established by digesting the appropriate CNBr fragment separately with trypsin, chymotrypsin, and thermolysin and sequencing the resulting peptides. The region from residues 70 to 120 was present in another CNBr fragment which was submitted directly to automatic Edman degradation. The result of this experiment extended the sequence to residue 100. The primary structure of the remaining portion of the VH region was determined by automatic Edman degradation of a lysine-blocked tryptic peptide derived from this region which included residues 98-214. The sequence of the VH region of New corresponds most closely to VH sequences of proteins in the VH II subgroup. This primary structure makes it possible to construct a model from the high-resolution electron-density map of protein New.

摘要

已确定人免疫球蛋白重链可变区的氨基酸序列。由于重链的氨基末端被封闭,通过分别用胰蛋白酶、胰凝乳蛋白酶和嗜热菌蛋白酶消化适当的溴化氰片段并对所得肽段进行测序,确定了第1至69位残基的序列。第70至120位残基所在的区域存在于另一个溴化氰片段中,该片段直接进行自动埃德曼降解。该实验结果将序列延伸至第100位残基。VH区其余部分的一级结构通过对源自该区域的赖氨酸封闭的胰蛋白酶肽段进行自动埃德曼降解来确定,该肽段包含第98至214位残基。New的VH区序列与VH II亚组中蛋白质的VH序列最为接近。这一一级结构使得能够根据蛋白质New的高分辨率电子密度图构建一个模型。

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