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以人工合成的多肽poly(Glu-Ala-Tyr)_(6:3:1)为底物测定了人外周血淋巴细胞膜酪氨酸蛋白激酶的活性,并对其性质进行了初步研究。发现Mg~(2+)对该酶的激活远远大于Mn~(2+),且Mg~(2+)最大激活浓度为50mmol/L左右。在5mg/ml的多肽底物浓度下,TPK达到最大反应速度,其Km值约为2.5mg/ml;对ATP、TPK的Km值大约为19μmol/L。多肽底物磷酸化氨基酸分析表明,仅有酪氨酸残基被磷酸化。
The activity of tyrosine protein kinase in human peripheral blood lymphocytes was assayed by the synthetic peptide poly (Glu-Ala-Tyr) _ (6: 3: 1) and its properties were studied. It was found that the activation of Mg ~ (2+) was far greater than that of Mn ~ (2+), and the maximum activation concentration of Mg ~ (2+) was about 50mmol / L. At a peptide substrate concentration of 5 mg / ml, TPK reached its maximum reaction rate with a Km of about 2.5 mg / ml; for Km of ATP, TPK was approximately 19 [mu] mol / L. Phosphorylation of polypeptide substrates Amino acid analysis showed that only tyrosine residues were phosphorylated.