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  • 标题:Primary structure of murine major histocompatibility complex alloantigens: Amino acid sequence studies of the cyanogen bromide fragments of the H-2Kb glycoprotein
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  • 作者:J. E. Coligan ; T. J. Kindt ; B. M. Ewenstein
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1978
  • 卷号:75
  • 期号:7
  • 页码:3390-3394
  • DOI:10.1073/pnas.75.7.3390
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Radiochemical microtechniques have been used in the amino acid sequence analysis of five major CNBr fragments of the glycoprotein specified by the murine major histocompatibility complex gene H-2kb. These fragments have been tentatively aligned and represent the NH2-terminal 80% of the intact molecule. All amino acids except Asp, Asn, and Gln have been assigned in 128 out of 149 possible positions in the NH2-terminal portions of each of these fragments. These assignments, which represent approximately 50% of the total sequence from these fragments, are listed below in the order of their alignment in the intact H-2Kb molecule: IIIn, -PHSLRYFVTAVSRP(G)L(G)(E)PRYM; IIIa, EVGYV--TEFVRF-S-AE(A)PRYEPR(A)--M; Ib, E-EGPEYWERET-KAK(G)-E-SFR--LRTLL(G)YY--TK; Ia, AALITK-KWE-AGEAERLRAYLEGTC-E-L; Ic, ELVETRPAG-GTF-KWAS-VVPLGKE-YY(T). The unassigned positions represented by dashes in the above sequences may be tentatively assigned as Asp, Asn, or Gln. The NH2-terminal sequence obtained for the H-2Kb molecule was compared to the limited sequence information available for other major histocompatibility complex gene products. An 84% homology (16 of 19 residues) to the H-2Kq and H-2Kk molecules, which are identical to one another in the positions compared, was observed. A similar comparison with 28 of the 31 NH2-terminal residues of HLA-B7 indicated 68% homology. Furthermore, significant homology was observed between H-Kb and HLA-B7 in a region of glycosylation, which occurs between positions 85 and 100 in the two molecules.
  • 关键词:histocompatibility antigens ; radiolabeling ; immunoprecipitation
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