Rabbit liver dCMP phosphohydrolase: a pyrimidine 5'-nucleotidase I-like enzyme in non-erythrocytic cells
| Autor: | Shin-ichiro Kawai, Shigeru Hokari, Toshiyuki Matsunaga, Takashi Miyazaki, Iwao Koyama, Tsugikazu Komoda |
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| Rok vydání: | 2003 |
| Předmět: |
Erythrocytes
Pyrimidine Physiology Blotting Western Cytidine Biology Biochemistry Catalysis 5'-nucleotidase Substrate Specificity chemistry.chemical_compound Western blot Nucleotidase medicine Animals Nucleotide Rats Wistar Molecular Biology 5'-Nucleotidase chemistry.chemical_classification medicine.diagnostic_test Gene Expression Profiling Hydrolysis Molecular biology Phosphoric Monoester Hydrolases Rats Cytosol Enzyme chemistry Liver Rabbits Liver Extracts |
| Zdroj: | Comparative biochemistry and physiology. Part B, Biochemistrymolecular biology. 134(2) |
| ISSN: | 1096-4959 |
| Popis: | A nucleotide phosphomonoesterase activity that preferably hydrolyzed dCMP was detected in rabbit liver and purified approximately 20-fold. The enzyme was similar in the catalytic and molecular properties to pyrimidine 5'-nucleotidase subclass I (P5N-I), which distributed specifically in vertebrate erythrocytes. In addition to liver, the activity was found in rabbit kidney, spleen, heart, intestine, but was not detected in any rat or chicken tissues tested. The rabbit enzyme protein reacted with antibodies against chicken P5N-I. Its pI was estimated to be approximately 5.3, and the enzyme was concluded to consist of single polypeptide of an approximately 38 kDa based on gel filtration and Western blot analysis. The partially purified enzyme preferentially hydrolyzes dCMP, UMP and CMP, K(m) values for these substrates are approximately 0.3 mM, the optimal pH is approximately 7, and the enzyme requires Mg(2+). This nucleotidase may contribute to the regulation of intracellular pyrimidine nucleotides in the rabbit. |
| Databáze: | OpenAIRE |
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