Keller J M, Keller K M
Department of Biological Chemistry and Structure, University of Health Sciences/The Chicago Medical School, IL 60064.
Biochim Biophys Acta. 1987 Nov 6;926(2):139-44. doi: 10.1016/0304-4165(87)90230-3.
The uptake of sulfate by Swiss mouse 3T3 cells is blocked in the presence of 1 mM 4-isothiocyano-4'-acetamido-stilbene-2,2-disulfonic acid (SITS). In the absence of an exogenous source of sulfate, glycosaminoglycans produced by cells in the presence of the inhibitor are sulfated to the same extent as those produced by cells grown in its absence. The sulfate utilized in the absence of medium sulfate has been identified as that produced by the oxidation of the sulfur present in the amino acids cysteine and methionine. This finding indicates that, under conditions of restricted exogenous sulfate, caution is needed in the interpretation of data obtained with the use of [35S]methionine and/or [35S]cysteine as a general protein label, since both tyrosine and a variety of types of protein-linked carbohydrate chains may be modified by sulfation.
在1 mM 4-异硫氰酸-4'-乙酰氨基芪-2,2-二磺酸(SITS)存在的情况下,瑞士小鼠3T3细胞对硫酸盐的摄取被阻断。在没有外源硫酸盐的情况下,在抑制剂存在下细胞产生的糖胺聚糖的硫酸化程度与在其不存在时生长的细胞产生的糖胺聚糖相同。在没有培养基硫酸盐的情况下利用的硫酸盐已被鉴定为半胱氨酸和蛋氨酸中存在的硫氧化产生的硫酸盐。这一发现表明,在外源硫酸盐受限的条件下,在解释使用[35S]蛋氨酸和/或[35S]半胱氨酸作为一般蛋白质标记获得的数据时需要谨慎,因为酪氨酸和各种类型的蛋白质连接的碳水化合物链都可能被硫酸化修饰。