David E, Shanmugam G
Cancer Biology Division, School of Biological Sciences, Madurai Kamaraj University, India.
Biochem Int. 1988 Dec;17(6):1039-47.
In vitro phosphorylation of brain proteins of developing chick embryos showed a drastic increase in the extent of phosphorylation of a 22 KDa protein from the fourteenth day reaching a peak at seventeenth day of development; the phosphorylation of the 22 KDa protein declined afterwards. Phosphoaminoacid analysis of the 22 KDa protein indicated serine residues as targets of phosphorylation. Isoelectric focusing followed by second dimensional SDS-PAGE indicated that the 22 KDa protein had a pI value of 4.5. Polymyxin B, an inhibitor of Ca2+ and phospholipid dependent protein kinases inhibited the phosphorylation of the 22 KDa protein.
发育中鸡胚脑蛋白的体外磷酸化显示,从第14天开始,一种22千道尔顿蛋白的磷酸化程度急剧增加,在发育的第17天达到峰值;此后,22千道尔顿蛋白的磷酸化水平下降。对该22千道尔顿蛋白的磷酸氨基酸分析表明,丝氨酸残基是磷酸化的靶点。等电聚焦后进行二维SDS-PAGE分析表明,该22千道尔顿蛋白的等电点值为4.5。多粘菌素B是一种Ca2+和磷脂依赖性蛋白激酶的抑制剂,它能抑制22千道尔顿蛋白的磷酸化。