Schrader W P, Woodward F J, Pollara B
J Biol Chem. 1979 Dec 10;254(23):11964-8.
A protein which specifically complexes with adenosine deaminase (complexing protein) has been purified to homogeneity from human plasma. This protein was compared with complexing protein isolated from human kidney. The two proteins produce electrophoretically different forms of high molecular weight adenosine deaminase when combined with the Mr = 36,000 enzyme monomer from erythrocytes. This difference may, at least in part, be due to the greater sialic acid content of complexing protein from plasma. By other criteria, including amino acid composition, total carbohydrate content, and subunit structure, the two proteins are quite similar. In addition, plasma complexing protein shows complete cross-reactivity with anti-kidney complexing protein serum. These results suggest that plasma and kidney complexing proteins are products of the same gene.
一种能与腺苷脱氨酶特异性结合的蛋白质(结合蛋白)已从人血浆中纯化至同质状态。将这种蛋白质与人肾中分离出的结合蛋白进行了比较。当这两种蛋白质与来自红细胞的分子量为36,000的酶单体结合时,会产生电泳形式不同的高分子量腺苷脱氨酶。这种差异可能至少部分归因于血浆中结合蛋白较高的唾液酸含量。根据其他标准,包括氨基酸组成、总碳水化合物含量和亚基结构,这两种蛋白质非常相似。此外,血浆结合蛋白与抗肾结合蛋白血清表现出完全的交叉反应性。这些结果表明,血浆和肾结合蛋白是同一基因的产物。