✦ LIBER ✦

Characteristics of galactokinase and galactose-1-phosphate uridyltransferase in cultivated fibroblasts and amniotic fluid cells

✍ Scribed by Yoon Shin-Buehring; H. Leitner; H. Henseleit; Antje Wirtz; Brigitte Haas; J. Schaub

Book ID: 104696804
Publisher: Springer
Year: 1979
Tongue: English
Weight: 345 KB
Volume: 48
Category: Article
ISSN: 0340-6717
DOI: 10.1007/bf00273271

No coin nor oath required. For personal study only.

✦ Synopsis

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.

📜 SIMILAR VOLUMES

Enzyme kinetics in mammalian cells. III.

Enzyme kinetics in mammalian cells. III. Regulation of activities of galactokinase, galactose-1-phosphate uridyl transferase and uridine diphosphogalactose-4-epimerase in human erythrocytes

✍ Helene Z. Hill 📂 Article 📅 1971 🏛 John Wiley and Sons 🌐 English ⚖ 874 KB

The sequential enzyme assay as previously described has been used to study various effects on the three enzymes in human red cells involved in the phosphorylation of galactose : galactokinase, galactose-1-phosphate uridyl transferase and uridine diphospho-galactose-4-epimerase. 1. Enzyme activities