Risnik V V, Dobrovolskii A B, Gusev N B, Severin S E
Biochem J. 1980 Dec 1;191(3):851-4. doi: 10.1042/bj1910851.
Rabbit skeletal-muscle troponin T was phosphorylated by a standard preparation of phosphorylase kinase [Cohen (1973) Eur. J. Biochem. 34, 1--14] and by fractions obtained after chromatography of phosphorylase kinase on phosphocellulose. The original preparation of phosphorylase kinase phosphorylated at least two sites, one of which was serine-1. The second and probably the third sites were presumably located in the peptide flanked by amino-acid residues 147 and 161 of troponin T. Fractions of phosphorylase kinase was adsorbed on phosphocellulose phosphorylated only the second site. Tightly adsorbed fractions possessed high troponin T kinase and phosvitin kinase activities and phosphorylated only serine-1 of troponin T. The results suggest that standard preparations of phosphorylase kinase are contaminated by troponin T kinase, which can phosphorylate serine-1 of troponin T.
兔骨骼肌肌钙蛋白T被磷酸化酶激酶的标准制剂[科恩（1973年），《欧洲生物化学杂志》34卷，1 - 14页]以及磷酸化酶激酶在磷酸纤维素上色谱分离后得到的组分磷酸化。磷酸化酶激酶的原始制剂使至少两个位点磷酸化，其中一个位点是丝氨酸 - 1。第二个位点可能还有第三个位点大概位于肌钙蛋白T中由氨基酸残基147和161侧翼的肽段中。吸附在磷酸纤维素上的磷酸化酶激酶组分仅使第二个位点磷酸化。紧密吸附的组分具有高肌钙蛋白T激酶和卵黄高磷蛋白激酶活性，并且仅使肌钙蛋白T的丝氨酸 - 1磷酸化。结果表明，磷酸化酶激酶的标准制剂被肌钙蛋白T激酶污染，该激酶可使肌钙蛋白T的丝氨酸 - 1磷酸化。
