1. Nucleoside monophosphoramidate hydrolase from rat liver: Purification and characterization
- Author
-
Okizaki Tsuyoshi, Kumon Akira, Kuba Masako, and Ohmori Hitoshi
- Subjects
chemistry.chemical_classification ,Hydrolases ,Chemistry ,Adenylyl Imidodiphosphate ,Hydrolysis ,Proteins ,Phosphoramidate ,Biochemistry ,Adenosine ,Rats ,Substrate Specificity ,Divalent ,Cytosol ,Liver ,Hydrolase ,Centrifugation, Density Gradient ,medicine ,Animals ,Rats, Wistar ,Ultracentrifugation ,Polyacrylamide gel electrophoresis ,Nucleoside ,medicine.drug - Abstract
1. Adenosine 5'-phosphoramidate hydrolase of 29 kDa was isolated from rat liver cytosol. 2. It consisted of two subunits of 14 kDa. 3. It hydrolyzed nucleoside 5'-monophosphoramidates into nucleoside 5'-monophosphates and ammonia, while it did not hydrolyze adenylyl phosphoramidate, adenylyl imidodiphosphate and N-phosphorylated compounds like phosphocreatine, N omega-phosphoarginine, 6-phospholysine and 3-phosphohistidine. 4. Divalent cations and cyclic AMP had no effect on the hydrolytic activity.
- Published
- 1994