Purification and properties of bovine uterine glutamic dehydrogenase: A comparison with the liver enzyme

Autor: Edward H. Frieden, Nancy C.Y. Lan, Allen B. Rawitch
Rok vydání: 1975
Předmět:
Zdroj: International Journal of Biochemistry. 6:871-874
ISSN: 0020-711X
DOI: 10.1016/0020-711x(75)90006-3
Popis: 1. 1. SPl-Glutamate dehydrogenase (GDH) has been isolated from cotyledons of pregnant bovine uterus. 2. 2. Although the specific activity of uterine GDH is relatively low, its enzymatic parameters are similar to those of the liver enzyme. 3. 3. The molecular weight of uterine GDH is approximately 240,000; unlike the liver enzyme, it does not display concentration-dependent aggregation. Alanine dehydrogenase activity is confined to a lower molecular weight (mol. wt = 160,000) form, which appears to be in rapid equilibrium with the larger species. 4. 4. The effects of nucleotides, steroid hormones, and diethylstilbestrol upon the enzymatic activity of uterine GDH have been examined.
Databáze: OpenAIRE