Primary structure of murine major histocompatibility complex alloantigens: completion of the sequence of the amino-terminal 284 residues of H-2Kb.
Primary structure of murine major histocompatibility complex alloantigens: completion of the sequence of the amino-terminal 284 residues of H-2Kb.
复制标题
鼠主要组织相容性复合物同种抗原的一级结构：完成 H-2Kb 氨基末端 284 个残基的序列。
DOI：
10.1021/bi00567a037
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发表时间：
1980
期刊：
影响因子：
2.9
通讯作者：
Nathenson,SG
中科院分区：
文献类型：
--
作者：
Martinko,JM;Uehara,H;Ewenstein,BM;Kindt,TJ;Coligan,JE;Nathenson,SG
John M.放大图片创作者：布鲁斯M.放大图片作者：托马斯J. Coligan和Stanley G. Nathenson* 摘要：完成了小鼠组织相容性抗原H-2Kb胞外部分羧基端溴化氰（CNBr）裂解片段Ic（CN-Ic）的一级结构。CN-1c含有木瓜蛋白酶裂解位点，该位点通过裂解分子的膜整合部分来溶解H-2Kb。用胰蛋白酶消化CN-Ic，用柠康酸酐封闭赖氨酸基团前后回收的肽段测定了CN-Ic的氨基酸序列。通过氨基末端序列分析获得胰蛋白酶片段的重叠序列。本文报道了小鼠H-2 Kb 1的Glu-Leu-Val-Glu-Thr-lidiochemical microsequencing技术，用于测定其蛋白质的一级结构。前173个残基的序列测定是在对CNBr片段、CN-IIIn、CN-IIIa和CN-Ib的一系列研究中完成的（Coligan等人，1978年、1979年;
John M. Martinko, Hiroshi Uehara, Bruce M. Ewenstein, Thomas J. Kindt, John E. Coligan, and Stanley G. Nathenson* abstract: The primary structure of the COOH-terminal cyanogen bromide (CNBr) cleavage fragmentIc (CN-Ic) of the extracellular portion of the murine histocompatibility antigen H-2Kb has been completed. CN-Ic contains a site of papain cleavage which has been utilized for solubilizing H-2Kb by cleaving off the membraneintegrating portion of the molecule. The amino acid sequence of CN-Ic has been de-termined by using peptides recovered after trypsin digestion of CN-Ic before and after blockage of lysine groups with citraconic anhydride. Overlapping sequences for the tryptic fragments were obtained by amino-terminal sequence analysis. The sequence of fragment CN-Ic, which spans residues 229-284 in H-2Kb, is as follows: Glu-Leu-Val-Glu-Thr-liadiochemical microsequencing techniques have been ap-plied to the murine H-2 alloantigen H-2Kb 1 as an approach to determining the primary structure of proteins available in amounts too small for classical sequencing analysis. Determination of thesequence of the first 173 residues was ac-complished in a series of studies on the CNBr fragments, CN-IIIn, CN-IIIa, and CN-Ib (Coligan et al., 1978, 1979;