TRYPTIC PEPTIDE COMPARISON OF IA ANTIGEN-ALPHA AND BETA-POLYPEPTIDES FROM THE I-A MUTANT B6.C-H-2BM12 AND ITS CONGENIC PARENTAL STRAIN B6
TRYPTIC PEPTIDE COMPARISON OF IA ANTIGEN-ALPHA AND BETA-POLYPEPTIDES FROM THE I-A MUTANT B6.C-H-2BM12 AND ITS CONGENIC PARENTAL STRAIN B6
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DOI：
10.1007/bf00344298
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发表时间：
1981-01-01
期刊：
影响因子：
3.2
通讯作者：
DAVID, C
中科院分区：
文献类型：
--
作者：
MCKEAN, DJ;MELVOLD, RW;DAVID, C
先前对 B6.C-H-2 bm12 (bm12) 品系的研究表明，小鼠 H-2 主要组织相容性复合体的 I-A 亚区存在突变。该突变导致 Ir 基因功能以及 Ia 和 MLR（混合淋巴细胞切除）决定因素的缺陷。 bm12突变体和亲本B6 Ia-抗原组分多肽的分子大小的比较未能证明α有任何差异。和.beta。多肽。因此，Ia.α中不存在主要的结构添加或缺失。和.beta。链多肽或碳水化合物结构。在 bm12 Ia 抗原制剂中一致观察到不变 (31K) 多肽的量显着减少。 14C B6 和 3H bm12 .alpha 的胰蛋白酶肽比较。和.beta。 bm12 .beta 中的多肽表现出有限数量的肽差异。多肽，但 bm12.alpha 中没有。多肽。这些生化突变和改变的生物现象的重要性将结合 Ia 抗原上的免疫相互作用位点模型进行讨论。
Previous studies of the B6.C-H-2 bm12 (bm12) strain demonstrated the presence of a mutation localized to the I-A subregion of the mouse H-2 major histocompatibility complex. This mutation is responsible for defects in Ir-gene function and in Ia and MLR (mixed lymphocyte resection) determinants. A comparison of the molecular size of the bm12 mutant and the parental B6 Ia-antigen component polypeptides failed to demonstrate any differences in the .alpha. and .beta. polypeptides. Thus, no major structural additions or deletions are present in the Ia .alpha. and .beta. chain polypeptide or carbohydrate structure. A significant decrease in the amount of invariant (31K) polypeptide was consistently observed in the bm12 Ia antigen preparations. Tryptic peptide comparisons of 14C B6 and 3H bm12 .alpha. and .beta. polypeptides demonstrated a limited number of peptide differences in the bm12 .beta. polypeptide but none in the bm12 .alpha. polypeptide. The significance of these biochemical mutations and altered biological phenomena are discussed in relation to a model of the immunological interaction sites on Ia antigens.