Kimball E S, Coligan J E
Mol Immunol. 1983 Jan;20(1):11-9. doi: 10.1016/0161-5890(83)90100-1.
The primary structure of the carboxy-terminal portion of the H-2Kd murine major histocompatibility antigen has been determined using radiosequencing methodology. The two peptides encompassing the entire cytoplasmic portion of the H-2Kd molecule were isolated from cyanogen bromide digests of the detergent solubilized molecule. These two peptides are not present in CNBr digests of papain-solubilized H-2Kd. Alignment of the two CNBr peptides was deduced from tryptic overlap peptides derived from the whole molecule. Alignment with the corresponding region of the H-2Kb antigen shows 90% homology and supports the assignment of this segment of H-2Kd as the C-terminal. The sequence obtained in this study is (Met)-Arg-Arg-Asn-Thr-Gly-Gly-Lys-Gly-Val-Asn-Tyr-Ala-Leu-Ala-Pro-Gly-Ser-Gln- Thr-Ser-Asp-Leu-Ser-Leu-Pro-Asp-Pro-Lys-Val-Met-Val-His-Asp-Pro-His-Ser-Leu- Ala. These data allow extensive comparisons with the protein sequences deduced from the 3' ends of H-2d haplotype cDNA and genomic clones as well as with the homologous regions of H-2Kb and H-2Db.
已使用放射性测序方法确定了H-2Kd小鼠主要组织相容性抗原羧基末端部分的一级结构。从去污剂溶解的分子的溴化氰消化物中分离出包含H-2Kd分子整个细胞质部分的两种肽。这两种肽不存在于木瓜蛋白酶溶解的H-2Kd的溴化氰消化物中。两种溴化氰肽的比对是从整个分子衍生的胰蛋白酶重叠肽推导出来的。与H-2Kb抗原相应区域的比对显示出90%的同源性，并支持将H-2Kd的这一区域指定为C末端。本研究获得的序列为(Met)-Arg-Arg-Asn-Thr-Gly-Gly-Lys-Gly-Val-Asn-Tyr-Ala-Leu-Ala-Pro-Gly-Ser-Gln-Thr-Ser-Asp-Leu-Ser-Leu-Pro-Asp-Pro-Lys-Val-Met-Val-His-Asp-Pro-His-Ser-Leu-Ala。这些数据允许与从H-2d单倍型cDNA和基因组克隆的3'末端推导的蛋白质序列以及与H-2Kb和H-2Db的同源区域进行广泛比较。
