Structure and evolution of transplantation antigens: partial amino-acid sequences of H-2K and H-2D alloantigens.

Structure and evolution of transplantation antigens: partial amino-acid sequences of H-2K and H-2D alloantigens.
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移植抗原的结构和进化:H-2K和H-2D同种抗原的部分氨基酸序列。

DOI:
10.1073/pnas.73.2.599
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发表时间:
1976
影响因子:
11.1
通讯作者:
L. Hood
L. Hood
中科院分区:
综合性期刊1区
文献类型:
--
作者:
J. Silver;L. Hood

文献摘要

被引文献

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用于亚纳摩尔量的多肽的氨基酸序列分析的技术已被应用于表征通过间接免疫沉淀从脾细胞分离的小鼠的β 2-微球蛋白和移植抗原。在β 2-微球蛋白的NH 2末端27个残基中鉴定出11个残基;所有残基均与其他物种β 2-微球蛋白相应位置上观察到的残基相同。对两种K和两种D移植抗原进行了检测,从有限的部分氨基酸序列数据中得出以下结论:(1)K和D分子彼此同源;(2)它们不显示与免疫球蛋白的氨基酸序列同源性;(3)两种K和两种D分子通过多个氨基酸取代而彼此不同;和(4)K分子作为一类不能与D分子作为一类区分开。遗传和进化的影响,这些意见进行了讨论。
Techniques for the amino acid sequence analysis of subnanomole quantities of polypeptides have been applied to characterize beta2-microglobulin and transplantation antigens of the mouse isolated from spleen cells by indirect immunoprecipitation. Eleven residues were identified throughout the NH2-terminal 27 residues of the beta2-microglobulin; all were identical to residues seen at the corresponding positions of beta2-microglobulins from other species. Two K and two D transplantation antigens were examined and the following generalizations emerged from the limited partial amino-acid sequence data: (1) the K and D molecules are homologous to one another; (2) they do not show amino acid sequence homology with immunoglobulins; (3) the two K and two D molecules differ from one another by multiple amino acid substitutions; and (4) the K molecules as a class cannot be distinguished from the D molecules as a class. The genetic and evolutionary implications of these observations are discussed.