Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The cytochemical localization of 5'-nucleotidase (5'-AMPase), and its validity, were investigated in parotid and submandibular acinar cells of a rat. Biochemical determinations showed that adequate treatment with glutaraldehyde could minimize the loss of enzymatic activity, and that 5'-AMPase and non-specific alkaline phosphatase (beta-GPase) possessed different pH optima. The cytochemical distribution of the reaction products from the 5'-AMPase activity was distinct from those of beta-GPase. 5'-AMPase activity was localized on the surface membranes of acinar, ductal and myoepithelial cells of both salivary glands. beta-GPase activity was evenly distributed on the entire plasma membranes of myoepithelial cells and on the basal plasmalemma of acinar cells. The reaction products, which appeared on the luminal and lateral plasma membranes of the acinar cells, were presumed to reflect the presence of 5'-AMPase, while those on the myoepithelial surface and basal plasma membranes of the acinar cells demonstrated both 5'-AMPase and beta-GPase. The results indicate that 5'-AMPase activity can be utilized as a reliable marker enzyme of plasma membranes in the salivary acinar cells.
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PMID:Cytochemical studies on the localization of 5'-nucleotidase in the acinar cells of the rat salivary glands. 3 29

The axon terminals of some capsaicin-sensitive sensory neurons in the spinal cord of the rat contain high amounts of acid phosphatase (EC 3.1.3.1) activity. We quantitated this activity in control and capsaicin-treated rats and mice in a biochemical assay using beta-glycerophosphate (beta-GP) and thiamine monophosphate (TMP), which have both been used in previous histological investigations, as substrates and measured the amount of phosphate liberated from particular fractions. The ventral spinal cord of rats yielded 209 +/- 9 (mean +/- S.E.M.) nmol phosphate/mg protein/h from beta-GP and 18 +/- 5 nmol from TMP; the values for the upper dorsal horn are 544 +/- 42 and 198 +/- 12 for beta-GP and TMP respectively. Values for mouse spinal cord tissue are quite similar; the spinal cord of guinea pigs contains lower amounts of beta-GPase and very little TMPase activity per mg protein. There was a fairly broad pH optimum between 5.4 and 6.3. After capsaicin (50 mg/kg s.c.) pretreatment, beta-GPase activity in the upper dorsal horn was decreased by 29% in rats and by 17% in mice; TMPase activity was reduced by 48% and 37% respectively. Values in the ventral spinal cord were unchanged. It is proposed that biochemical measurement of TMPase activity might be useful in quantitative investigations of acid phosphatase activity (e.g. "FRAP") in capsaicin-sensitive sensory neurons.
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PMID:Quantitative assay of capsaicin-sensitive thiamine monophosphatase and beta-glycerophosphatase activity in rodent spinal cord. 284 42

The characteristics of nonspecific alkaline phosphatase, (APase, EC 3.1.3.1.) measured as beta-glycerophosphatase (GPase, EC 3.1.3.1.), inorganic pyrophosphatase (PPiase, EC 3.6.1.1.) and adenosine triphosphatase (ATPase, EC 3.6.1.3.) were studied in detail of butanol extracts prepared from rat molar cementum. Mg2+ was not absolutely essential to any of the activities, but at low levels was stimulatory in all cases. Higher concentrations were inhibitory. Ca2+ stimulated ATPase activity weakly at low levels, but was slightly inhibitory to the other enzyme activities. All enzyme activities showed nearly identical sensitivities to heat inactivation and to L-p-bromotetramisole and levamisole, which caused nearly complete inhibition. About 10-15% of the ATPase activity was insensitive to L-p-bromotetramisole and levamisole. The data are consistent with the concept that GPase, PPiase and ATPase activities of cementum to a major part stem from one enzyme, namely nonspecific alkaline phosphatase.
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PMID:Properties of alkaline phosphatases from cellular cementum of rat molars. 612 76