Moreno C, Lundblad A, Kabat B A
J Exp Med. 1971 Aug 1;134(2):439-57. doi: 10.1084/jem.134.2.439.
The immunochemical properties of purified A(1) and A(2) glycoproteins have been compared to ascertain whether their antigenic determinants differ. Quantitative precipitin and complement-fixation studies using several anti-A sera as well as purified gammaG anti-A antibodies clearly showed a specificity difference. This was also supported by absorption studies: A(2) substance specifically removed antibodies reacting with A(2) substance leaving anti-A(1) activity. A(1) substance was more effective than A(2) substance in dissolving an A(1) anti-A(1)-specific precipitate. Purified gammaM anti-A hemolyzed A(1) cells more readily than A(2) cells. Inhibition studies using mono- and difucosyl type 2 A-active oligosaccharides showed that type 2 difucosyl receptors are present in A(2) substance. The structural basis for the specificity difference between A(1) and A(2) would appear to be that A(2) substances lack type 1 A determinants; this would account for the observed higher H and Le(b) activity in A(2) substances.
已对纯化的A(1)和A(2)糖蛋白的免疫化学特性进行了比较,以确定它们的抗原决定簇是否不同。使用几种抗A血清以及纯化的γG抗A抗体进行的定量沉淀和补体结合研究清楚地显示出特异性差异。吸收研究也支持了这一点:A(2)物质特异性去除了与A(2)物质反应的抗体,留下了抗A(1)活性。A(1)物质在溶解A(1)抗A(1)特异性沉淀物方面比A(2)物质更有效。纯化的γM抗A比A(2)细胞更容易使A(1)细胞溶血。使用单岩藻糖基和二岩藻糖基2型A活性寡糖的抑制研究表明,2型二岩藻糖基受体存在于A(2)物质中。A(1)和A(2)之间特异性差异的结构基础似乎是A(2)物质缺乏1型A决定簇;这可以解释在A(2)物质中观察到的较高的H和Le(b)活性。