Polynucleotidase activity of animal and plant tissue phosphodiesterases
| Autor: | W. E. Razzell |
|---|---|
| Rok vydání: | 1968 |
| Předmět: |
Hot Temperature
Phosphoric monoester hydrolases Swine Biology Kidney medicine.disease_cause RNA Transfer Nucleotidases Microsomes Escherichia coli medicine Animals Magnesium Binding site Edetic Acid chemistry.chemical_classification Carbon Isotopes Binding Sites Nucleotides Venoms Phosphodiesterase Snakes General Medicine Hydrogen-Ion Concentration NAD Phosphoric Monoester Hydrolases Kinetics medicine.anatomical_structure Enzyme Liver Biochemistry chemistry Microsome NAD+ kinase Plants Edible |
| Zdroj: | Canadian Journal of Biochemistry. 46:1-7 |
| ISSN: | 0008-4018 |
| DOI: | 10.1139/o68-001 |
| Popis: | The purification of phosphodiesterase I from hog liver has permitted the demonstration that its properties and catalytic activity are the same as the enzyme previously purified from kidney. The liver, kidney, and snake venom phosphodiesterase I preparations have been compared on the basis of their ability to hydrolyze p-nitrophenyl esters of the 5′-phosphates of thymidine, uridine, and deoxyadenosine at pH 9 in the absence of EDTA versus the activity of potato nucleotide pyrophosphatase, which is active at pH 7 in the presence of EDTA. Kidney microsomes are similarly inactive at the lower pH. Further, the tissue and venom enzymes possess activity against pTpT, TpT, and ribooligonucleotides which are not attacked by the plant nucleotide pyrophosphatase.A comparison of the loss of activity during heating, rates of hydrolysis, kinetics, and competitive inhibition of the animal tissue phosphodiesterase I on several substrates indicates that one catalytic site is responsible for the cleavage of nucleoside 5′-phosphate from p-nitrophenyl esters, TppT, and NAD+. The tissue enzyme, like the venom enzyme, is active on the 3′-hydroxyl terminus of transfer RNA. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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