摘要
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。
In this paper, with poly (Glu-Ala-Tyr)6:8:1, a defined tyrosine-spe-cific substrate, the activity of TPK in human peripheral blood lymphocyte membrane was quantitated. The properties of the enzyme were preliminarily characterized. The results indicated that the stimulation of Mg2+ to the enzyme was much higher than that of Mn2+ , and the best stimulating concentration of Mg2+ was about 50 mmol/L. The activity of the enzyme reached its maximum when the concentraion of the polymer rose to 5 mg/ ml. For the polymer, the Km value of the enzyme was about 2.5mg/ml, and for ATP, the Km value was about 19umol/L.
出处
《徐州医学院学报》
CAS
1990年第2期99-105,共7页
Acta Academiae Medicinae Xuzhou
