Lou L L, Clarke S
Biochem J. 1986 Apr 1;235(1):183-7. doi: 10.1042/bj2350183.
The anion transport protein of the human erythrocyte membrane, band 3, is reversibly methylated by an endogenous protein carboxyl methyltransferase. The physiological consequence of this modification was studied by measuring the rate of phosphate transport by intact erythrocytes incubated under conditions where protein methylation reactions are inhibited. No change in phosphate transport was detected when cells were treated with either methionine-free media or cycloleucine, whereas cells incubated with adenosine and homocysteine thiolactone displayed a marginally slower rate of transport, which was not reversed by subsequent remethylation of the membrane proteins. These results suggest that erythrocyte protein carboxyl methylation does not directly regulate this activity of band 3.
人类红细胞膜的阴离子转运蛋白带3可被一种内源性蛋白质羧基甲基转移酶可逆地甲基化。通过测量在蛋白质甲基化反应受到抑制的条件下孵育的完整红细胞的磷酸盐转运速率,研究了这种修饰的生理后果。当细胞用无蛋氨酸培养基或环亮氨酸处理时,未检测到磷酸盐转运的变化,而用腺苷和同型半胱氨酸硫内酯孵育的细胞显示出略微较慢的转运速率,膜蛋白随后的再甲基化并不能逆转这种速率。这些结果表明,红细胞蛋白质羧基甲基化并不直接调节带3的这种活性。