The phosphorylation of the major proteins of the human erythrocyte membrane.
The phosphorylation of the major proteins of the human erythrocyte membrane.
复制标题
人红细胞膜主要蛋白质的磷酸化。
DOI：
10.1016/0003-9861(79)90356-4
复制
发表时间：
1979
影响因子：
3.9
通讯作者：
L. Waxman
中科院分区：
文献类型：
--
作者：
L. Waxman
主要的唾液酸糖蛋白（PAS-1）和Fairbankset等人命名的组分都是唾液酸糖蛋白。（G.费尔班克斯，T. L. Steck和D. F. H. Wallach，1971，Biochemistry 10，2606-2617）作为条带3，由于存在共价结合的丝氨酸和苏氨酸磷酸残基，显示为真正的磷蛋白。与其他研究结果一致，当鬼与[γ-32 P]ATP孵育时，PAS-1似乎不被磷酸化，但当细胞与32 Pi孵育时，PAS-1的磷酸化是显著的（约0.15 mol/mol）。带3被磷酸化至0.90 mol/mol的程度，并且这些位点明显地分布在沿着多肽链的几个位置。Spectrin也是一种磷蛋白，每450，000道尔顿蛋白质含有约4个磷酸分子。这三种多肽的磷酸化不受cAMP存在的刺激。
Both the major sialoglycoprotein (PAS-1) and the component designated by Fairbankset al.(G. Fairbanks, T. L. Steck, and D. F. H. Wallach, 1971,Biochemistry10, 2606–2617) as Band 3 are shown to be bonafide phosphoproteins by virtue of the presence of covalently bound serine and threonine phosphate residues. In agreement with the findings of others, PAS-1 does not seem to be phosphorylated when ghosts are incubated with [γ-32P]ATP, but the phosphorylation is significant (about 0.15 mol/mol) when the cells are incubated in the presence of32Pi. Band 3 is phosphorylated to the extent of 0.90 mol/mol, and these sites are apparently distributed in several places along the polypeptide chain. Spectrin is also a phosphoprotein containing approximately four molecules of phosphate per 450,000 daltons of protein. The phosphorylation of these three polypeptides is not stimulated by the presence of cAMP.