Kudlicki W, Grankowski N, Gasior E
Eur J Biochem. 1978 Mar 15;84(2):493-8. doi: 10.1111/j.1432-1033.1978.tb12191.x.
Three fractions of protein kinase from postribosomal supernatant of Saccharomyces cerevisiae, active in phosphorylation of casein, were resolved on DEAE-cellulose. Two of these fractions: protein kinase 1 and protein kinase 3, were further purified about 1000 and 1800-fold respectively. The kinase 1 appeared to exist as a monomer with a molecular weight of 50 000 and utilized only ATP as phosphoryl donor. The protein kinase 3 was an aggregated form of enzyme with a molecular weight of above half a million and used both ATP and GTP for protein phosphorylation. Both isolated enzymes showed variations in respect to Michaelis constants, and inhibitory effects exerted by monovalent cations and nucleotide phosphates. The activity of the kinases was not affected by the presence of cAMP (adenosine 3':5'-monophosphate) or cGMP, however, only protein kinase 1 appeared to be a cAMP nucleotide-independent enzyme. Despite these differences both enzymes equally phosphorylated two strongly acidic proteins of the 60-S ribosome subunit, possibly related to L7, L12 of Escherichia coli.
对酿酒酵母核糖体后上清液中具有酪蛋白磷酸化活性的三种蛋白激酶组分在二乙氨基乙基纤维素上进行了分离。其中两种组分：蛋白激酶1和蛋白激酶3，分别进一步纯化了约1000倍和1800倍。激酶1似乎以分子量为50000的单体形式存在，并且仅利用ATP作为磷酰基供体。蛋白激酶3是一种分子量超过50万的酶聚集体形式，并且使用ATP和GTP进行蛋白质磷酸化。两种分离出的酶在米氏常数、单价阳离子和核苷酸磷酸的抑制作用方面均表现出差异。激酶的活性不受环磷酸腺苷（3':5'-单磷酸腺苷）或环磷酸鸟苷的影响，然而，只有蛋白激酶1似乎是一种不依赖环磷酸腺苷核苷酸的酶。尽管存在这些差异，但两种酶均能同等程度地磷酸化60-S核糖体亚基的两种强酸性蛋白，这两种蛋白可能与大肠杆菌的L7、L12相关。
