酿酒酵母中的钙调蛋白依赖性蛋白激酶

Ca2+/calmodulin-dependent protein kinase in Saccharomyces cerevisiae.

作者信息

Londesborough J, Nuutinen M

出版信息

FEBS Lett. 1987 Jul 13;219(1):249-53. doi: 10.1016/0014-5793(87)81226-7.

Abstract

Ca2+-dependent chromatography of soluble cytosolic proteins on calmodulin-Sepharose gave a fraction that exhibited Ca2+- and calmodulin-dependent phosphorylation of several polypeptides, including 60, 56 and 45 kDa species. At 0.2 microM beef calmodulin the phosphorylation was optimal at 3 microM free Ca2+, and at 80 microM free Ca2+ it was half-maximal at about 0.1 microM beef calmodulin. It is concluded that the fraction contains calmodulin-dependent protein kinase(s) which is (are) autophosphorylated or associated with substrates.

摘要

将可溶性胞质蛋白在钙调蛋白-琼脂糖上进行钙依赖性层析，得到一个组分，该组分对几种多肽（包括60 kDa、56 kDa和45 kDa的蛋白）表现出钙和钙调蛋白依赖性磷酸化。在0.2 μM牛钙调蛋白存在下，磷酸化在3 μM游离钙时达到最佳，而在80 μM游离钙时，在约0.1 μM牛钙调蛋白时磷酸化达到最大值的一半。得出的结论是，该组分含有自磷酸化或与底物相关的钙调蛋白依赖性蛋白激酶。