Marais R M, Nguyen O, Woodgett J R, Parker P J
Ludwig Institute for Cancer Research, London, UK.
FEBS Lett. 1990 Dec 17;277(1-2):151-5. doi: 10.1016/0014-5793(90)80831-3.
The substrate specificity of purified PKC-alpha, -beta and -gamma has been investigated. A series of synthetic peptides based upon the sequence surrounding serine-7 in glycogen synthase were generated and used to determine the basic residue requirements of these PKC isotypes. While PKC-alpha and -beta are indistinguishable in their phosphorylation of these peptides, PKC-gamma shows a distinct specificity profile for these synthetic substrates.
已对纯化的蛋白激酶C-α、-β和-γ的底物特异性进行了研究。基于糖原合酶中丝氨酸-7周围序列生成了一系列合成肽,并用于确定这些蛋白激酶C同工型的碱性残基需求。虽然蛋白激酶C-α和-β对这些肽的磷酸化作用无法区分,但蛋白激酶C-γ对这些合成底物表现出明显不同的特异性特征。