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来自小鼠主要组织相容性复合体I-A亚区的Ia分子中的一种变异α链:一种可能的基因内重组。

A variant alpha-chain in an Ia molecule from the I-A subregion of the mouse major histocompatibility complex: a possible intragenic recombination.

作者信息

Rose S M, Cullen S E

出版信息

J Immunol. 1981 Oct;127(4):1472-7.

PMID:6792275
Abstract

The recombinant MHC haplotype t1, present in mouse strain A.TL and B10.TL, encodes an I-A molecule with a variant alpha-chain that was recognized when tryptic peptide digests from t1 and the nominal parental haplotype (a1 or k) were compared by double-label reverse phase HPLC. The t1 I-A alpha-chain possesses a tryptic peptide absent from a1 and k I-A alpha-chains, and lacks several peptides present in a1 and k. The peptide that differs in t1 is not a mannose-bearing peptide, and thus its altered mobility is probably not due to carbohydrate modification. The alteration in t1 could result from mutation or intragenic recombination, but the unique t1 peptide migrates in a position identical to a peptide found in haplotype s, a partner in the (s X a1) cross that generated the t1 recombinant. If this apparently shared peptide indicates an intragenic recombination, this places the I-A alpha-gene centromeric to the other I-A subregion gene, and together with the data of Jones, suggests a gene order of I-A alpha, I-A beta, I-E beta (A alpha, A beta, Ae).

摘要

存在于小鼠品系A.TL和B10.TL中的重组MHC单倍型t1编码一种具有变异α链的I-A分子,当通过双标记反相高效液相色谱法比较t1和标称亲本单倍型(a1或k)的胰蛋白酶肽消化产物时,该变异α链能够被识别。t1 I-Aα链拥有一条a1和k I-Aα链所没有的胰蛋白酶肽,并且缺少a1和k中存在的几条肽。t1中不同的肽不是含甘露糖的肽,因此其迁移率的改变可能不是由于碳水化合物修饰。t1中的改变可能是由突变或基因内重组导致的,但独特的t1肽的迁移位置与单倍型s中发现的一种肽相同,s是在产生t1重组体的(s×a1)杂交中的一个亲本。如果这种明显共享的肽表明存在基因内重组,这就将I-Aα基因定位在其他I-A亚区域基因的着丝粒侧,并且与琼斯的数据一起,提示了I-Aα、I-Aβ、I-Eβ(Aα、Aβ、Ae)的基因顺序。

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