Hiraga K, Tahara H, Taguchi N, Tsuchiya E, Fukui S, Miyakawa T
Department of Fermentation Technology, Faculty of Engineering, Hiroshima University, Japan.
J Gen Microbiol. 1991 Jan;137(1):1-4. doi: 10.1099/00221287-137-1-1.
Plasma membrane Ca2(+)-ATPase of Saccharomyces cerevisiae was solubilized and partially purified by calmodulin-affinity chromatography. The activity of Ca2(+)-ATPase isolated from MATa cells was inhibited by physiological concentrations of the mating pheromone alpha-factor in a dose-dependent manner. The enzyme prepared from a receptor-deficient sterile mutant cells (delta ste-2) was similarly inhibited by alpha-factor, but the enzyme from MAT alpha cells was resistant to the mating pheromone. We suggest that the inhibition may be involved in the alpha-factor-induced increase of Ca2+ uptake reaction of MATa cells.
酿酒酵母的质膜Ca2(+)-ATP酶通过钙调蛋白亲和层析法进行溶解和部分纯化。从MATa细胞中分离出的Ca2(+)-ATP酶的活性受到生理浓度的交配信息素α-因子的抑制，且呈剂量依赖性。从受体缺陷型无菌突变细胞（delta ste-2）制备的酶同样受到α-因子的抑制，但来自MATα细胞的酶对交配信息素具有抗性。我们认为这种抑制作用可能与α-因子诱导的MATa细胞Ca2+摄取反应增加有关。
