Shin-Buehring Y, Leitner H, Henseleit H, Wirtz A, Haas B, Schaub J
Hum Genet. 1979 Apr 17;48(1):31-7. doi: 10.1007/BF00273271.
The kinetic characteristics of galactose-1-phosphate uridyltransferase and galactokinase in cultivated fibroblasts and amniotic fluid cells were investigated. The Km values of galactokinase for galactose at 2.0 mM ATP are 0.34 mM in amniotic fluid cells and 0.48 mM in fibroblasts. The Km values for ATP at 0.5 mM galactose are 1.25 mM and 2.10 mM. Transferase and galactokinase activities and protein content increase logarithmically during the growth of cultivated cells. The specific activity of both enzymes also increases and reaches a maximum level 10--15 days after subculture. The specific activity of transferase increases faster than that of galactokinase in the case of amniotic fluid cells. In the case of fibroblasts the specific activity of galactokinase increases faster than that of transferase.
研究了培养的成纤维细胞和羊水细胞中1-磷酸半乳糖尿苷转移酶和半乳糖激酶的动力学特性。在2.0 mM ATP条件下，羊水细胞中半乳糖激酶对半乳糖的Km值为0.34 mM，成纤维细胞中为0.48 mM。在0.5 mM半乳糖条件下，对ATP的Km值分别为1.25 mM和2.10 mM。在培养细胞生长过程中，转移酶和半乳糖激酶活性以及蛋白质含量呈对数增加。两种酶的比活性也增加，并在传代培养10 - 15天后达到最高水平。在羊水细胞中，转移酶的比活性比半乳糖激酶增加得更快。在成纤维细胞中，半乳糖激酶的比活性比转移酶增加得更快。
