Michaelson J, Flaherty L, Bushkin Y, Yudkowitz H
Immunogenetics. 1981;14(1-2):129-40. doi: 10.1007/BF00344306.
The Qa-2 differentiation alloantigen is coded by a gene situated between the D and Tla loci of the murine major histocompatibility complex (H-2). Qa-2-bearing protein was isolated by immunoprecipitation and found to be composed of subunits of 40 000 and 12 000 daltons by SDS polyacrylamide gel electrophoresis (PAGE). The 12 000 dalton material was identified as beta 2-microglobulin (beta 2M) by its molecular weight (SDS PAGE), charge (isoelectric focusing), antigenicity (reactivity with xenogenic anti-beta 2M), and genetics. The 40 000 dalton mol. wt. of Qa-2 heavy chains is 5 000 daltons less than that of D and K molecules (45 000 daltons). The quantity of Qa-2 isolated by immunoprecipitation was found to vary in strain-specific fashion and as much as a 15-fold difference was observed.
Qa-2分化同种异体抗原由位于小鼠主要组织相容性复合体(H-2)的D和Tla基因座之间的一个基因编码。通过免疫沉淀分离出携带Qa-2的蛋白质,经十二烷基硫酸钠聚丙烯酰胺凝胶电泳(PAGE)发现其由40000道尔顿和12000道尔顿的亚基组成。通过其分子量(SDS PAGE)、电荷(等电聚焦)、抗原性(与异种抗β2微球蛋白的反应性)和遗传学,将12000道尔顿的物质鉴定为β2微球蛋白(β2M)。Qa-2重链的40000道尔顿分子量比D和K分子(45000道尔顿)的分子量小5000道尔顿。发现通过免疫沉淀分离的Qa-2的量以菌株特异性方式变化,观察到的差异高达15倍。