Complete amino acid sequence of a papain-solubilized human histocompatibility antigen HLA-B7. 1. Isolation and amino acid composition of fragments and of tryptic and chymotryptic peptides.
Complete amino acid sequence of a papain-solubilized human histocompatibility antigen HLA-B7. 1. Isolation and amino acid composition of fragments and of tryptic and chymotryptic peptides.
复制标题
木瓜蛋白酶溶解的人组织相容性抗原 HLA-B7 的完整氨基酸序列。
作者：
J. A. López de Castro;H. Orr;R. Robb;T. Kostyk;D. Mann;J. Strominger
作为确定人组织相容性抗原HLA-B7重链木瓜蛋白酶溶解部分的完整共价结构的总体策略的一部分，通过部分酸水解和溴化氰切割的组合将蛋白质切割成各种片段。在通过色谱程序纯化后，这些片段已被用作胰蛋白酶和胰凝乳蛋白酶肽的来源。33个主要胰蛋白酶和22个主要胰凝乳蛋白酶肽纯化纳摩尔量和它们的氨基酸组成测定。除了氨基末端的CNBr五肽外，这些肽占多肽链的整个范围。它们为分子的酸裂解和溴化氰片段的正式比对提供了基础，也为阐明HLA-B7重链的一级结构提供了源材料。
As a part of the overall strategy for determining the complete covalent structure of the papain-solubilized portion of the heavy chain of the human histocompatibility antigen HLA-B7, the protein was dissected into various fragments by a combination of partial acid hydrolysis and cyanogen bromide cleavage. After purification by chromatographic procedures, these fragments have been used as a source for tryptic and chymotryptic peptides. Thirty-three major tryptic and twenty-two major chymotryptic peptides were purified in nanomole amounts and their amino acid compositions determined. These peptides account for the whole extent of the polypeptide chain with the exception of the amino-terminal CNBr pentapeptide. They provide the basis for the formal alignment of the acid cleavage and cyanogen bromide fragments of the molecule as well as the source material for the elucidation of the primary structure of the HLA-B7 heavy chain.