Nuutinen M, Londesborough J
Research Laboratories, Alko Ltd., Helsinki, Finland.
Second Messengers Phosphoproteins. 1988;12(4):197-205.
A casein kinase II that is tightly bound to yeast ribosomes was partially purified and used to phosphorylate YL 44 and an unidentified 36 kDa protein in purified ribosomes. At typical cytosolic salt concentrations the phosphorylation was strongly stimulated by moderate concentrations (200 microM) of spermine or spermidine. The lowest effective concentration of spermine (20 microM, causing less than 50% stimulation) was close to that of total spermine reported in nongrowing yeast. Increases in free polyamines accompanying the 10-fold increase in total spermine and spermidine in growing yeast may therefore significantly stimulate this phosphorylation.
一种与酵母核糖体紧密结合的酪蛋白激酶II被部分纯化，并用于使纯化核糖体中的YL 44和一种未鉴定的36 kDa蛋白质磷酸化。在典型的胞质盐浓度下，适度浓度（200 microM）的精胺或亚精胺能强烈刺激磷酸化作用。精胺的最低有效浓度（20 microM，刺激作用小于50%）接近非生长酵母中报道的总精胺浓度。因此，在生长酵母中总精胺和亚精胺增加10倍时伴随的游离多胺增加可能会显著刺激这种磷酸化作用。
