Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.4.37 (CNPase)
 539 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The properties of three phosphatases from Salmonella typhimurium have been examined. A cyclic 2',3'-nucleotide phosphodiesterase (EC 3.1.4.d) hydrolyzes cyclic 2',3'-purine and -pyrimidine nucleotides, as well as 3'-mononucleotides, and has a pH optimum of about 7.5. It requires divalent cations for activity and has a molecular weight of 67,000. Acid hexose phosphatase (EC 3.1.2.2) possesses activity towards hexose phosphates as well as other sugar phosphates. The enzyme is apparently a dimer of 37,000-dalton subunits. Nonspecific acid phosphatase (EC 3.1.3.2) hydrolyzes a variety of phosphate esters, including nucleotides and sugar phosphates. The enzyme also hydrolyzes the phosphoric anhydride bonds of pyrophosphate and nucleotides. Michaelis constants of the nonspecific acid phosphatase for several of its substrates are in the 1 to 2 mM range. Nonspecific acid phosphatase is a dimer of 27,000-dalton subunits.
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PMID:Properties of two phosphatases and a cyclic phosphodiesterase of Salmonella typhimurium. 1 82

The effect of methylnitrosourea (MNU) on cerebellar and cerebral DNA, RNA, protein, lysosomal enzymes (acid DNase, RNase, phosphatase, and beta-glucuronidase), and 2',3'-cyclic nucleotide 3'-phosphohydrolase (2',3'-CNPase) activities was studied in rats from birth through 12 days of age. Subcutaneous injection of MNU in a dose of 0.625 mmol/kg caused a suppression of increase in weights and content of DNA, RNA, and protein of cerebellum, but no changes in those of the cerebrum or in body weight. Ratios of protein and RNA to DNA were substantially elevated by MNU in the cerebellum but not in the cerebrum. Acid DNase and acid RNase activities of MNU-treated rats were significantly elevated beyond the increase of these activities in controls in the cerebellum, but no change in these activities by MNU was observed in the cerebrum. A slight elevation in acid phosphatase activity was observed in the cerebellum but not in the cerebrum after MNU pretreatment. Beta-glucuronidase and 2',3'-CNPase activities were not changed in the cerebellum or in the cerebrum. These results suggest that in the developing brain, especially in the cerebellum at the mitotic stage, MNU caused cell damage and inhibited cell mitosis.
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PMID:Cytotoxic effects of methylnitrosourea on developing brain. 619 99

A histochemical method for demonstration of 2',3'-cyclic nucleotide 3'-phosphohydrolase activity is proposed. Cryostat sections, fixed in chlorophorm-methanol mixture, are incubated in a solution containing cyclic adenosine 2',3'-monophosphate, acid phosphatase, lead nitrate in acetate buffer, pH = 6,4 or 6.5. This method is based on conversion by the 2',3'-cyclic nucleotide 3'-phosphohydrolase of cyclic adenosine 2',3'-monophosphate to nucleotide-2'-monophosphate. Under the action of exogenous acid phosphatase, inorganic phosphate is released. It precipitates as lead phosphate if lead ions are present. By adding yellow ammonium sulphide, the lead phosphate is converted to lead sulphide which is the visible reaction product.
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PMID:A histochemical method for demonstration of 2',3'-cyclic 3'-phosphohydrolase activity. 630 41

1. Neonatal mice received subcutaneous injections of buffer, thiourea (TU) or propylthiouracil (PTU). 2. The PTU-treated mice were sacrificed on postnatal day 14 (P14) and the TU-treated mice on P28. 3. Brain weights of the TU- and PTU-treated mice were not significantly different from the controls. 4. Acid but not alkaline phosphatase activity in the brainstem decreased after TU and PTU treatment. 5. Myelination as indicated by intensity of luxol fast blue staining was weaker in the drug-treated animals. 6. The level of myelin marker enzyme, 2',3'-cyclic nucleotide 3'-phosphohydrolase, was lower in the brainstem of PTU-treated animals. 7. The results suggest a correlation between acid phosphatase but not alkaline phosphatase activity with myelination in the developing mouse brain.
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PMID:Correlation of acid phosphatase but not alkaline phosphatase activity with myelination in the developing mouse brain. 838 67