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

A brush border preparation from rat intestine was incubated with rat intrinsic factor-vitamin B12 complex in 0.01 M Tris-HCl buffer, pH 7.4. The 57Co-B12 uptake to brush borders was proportional to the amount of protein or to alkaline phosphatase activity in the preparations. The uptake increased with time of incubation. At 37degreesC, the uptake after incubation for 15 min was 80-85% of that for one hr. The uptake at 4degreesC was approximately 70% of that at 37degreesC. Ther was no difference as a result of adding glucose to the incubation medium. The uptake was observed in the alkaline environment above pH 6.3. Maximum uptake occurred at pH 8.0. Brush borders washed with Krebs-Ringer bicarbonate buffer (pH 7.4) exhibited no difference in B12 uptake, whether in the presence or absence of calcium ion. But brush borders washed with ethylenediaminetetraacetate exhibited no uptake when incubated in calcium-free medium. The uptake reached a maximum by addition of calcium ion at a concentration of 0.3 mM, and was not alter up to 10 mM. Addition of magnesium ion exhibited no uptake. Calcium-dependent B12 uptake was markedly inhibited by manganese ion. Magnesium ion seemed to slightly inhibit the calcium-dependent uptake.
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PMID:Effects of divalent cations on vitamin B12 adsorption to brush borders of rat intestine. 0 95

A membrane fraction from calf thymocytes was used to investigate molecular and catalytic properties of membrane-bound alkaline phosphatase (ortho-phosphoric-monoester phosphohydrolase EC 3.1.3.1). The principal findings were: 1. Solubilization of membranes with the non-ionic detergent Triton X-100 increases alkaline phosphatase activity by 30-40%. The enzyme activity elutes in a single peak (Stokes' radius = 7.7 nm) after chromatography in Sepharose 6B in the presence of Triton X-100. The activity also sediments as a single component of approx. 6.4 S during centrifugation in sucrose gradients containing Triton X-100. 2. Ion-exchange chromatography and isoelectric focusing in the presence of Triton X-100 indicate substantial charge heterogeneity. Two overlapping bands, a peak at pH 5.92 with a pronounced shoulder at pH 5.29, are apparent by isoelectric focusing. 3. The pH optimum for hydrolysis of p-nitrophenylphosphate (pNPhP) by the undissolved enzyme(s) is 9.57. Half-maximal activity occurs at pH 8.65 and ph 10.45. Triton X-100 has no effect on the pH profile. 4. Catalytic activity is affected by amines, especially analogues of ethanolamine. Diethanolamine exerts a unique stimulatory effect, but does not change the pH dependency. Increasing the concentration of diethanolamine from 0 to 1 M causes a 6-fold increase in Km and a 10-fold increase in the rate of hydrolysis of pNPhP. Glycine is inhibitory. 5. EDTA causes an irreversible loss of activity with t1/2 (1 mM EDTA, pH 8.2, 23 degrees C) = 3.5 h. Optimal activity is achieved in 0.1--1.0 mM Mg2+, although this does not cause the degree of activation reported to occur with the purified enzymes. Other divalent ions are inhibitory. Concentrations required to reduce activity to 50% of control are: Zn2+, 4.0 muM (no added Mg2+) and 30 muM (in the presence of 1 mM Mg2+); Mn2+, 0.25 mM (+/- Mg2+); Ca2+, 20 mM (+/- Mg2+). 6. Monovalent cations have little effect on activity. In the absence of added Mg2+, 50--150 mM Na+ is partially inhibitory, but markedly less so in the presence of 1 mM Mg2+. K+ has no significant effect. 7. Of the substrates tested, pNPhP (Km = 44 muM) was most rapidly hydrolyzed. Other substrates (rate relative to pNPhP) were alpha-naphthylphosphate (0.79), 2'-AMP (0.80), 5'-AMP (0.70), 3'-AMP (0.63), alpha-glycerophosphate (0.47) and glucose 6-phosphate (0.35). Phosphodiesterase activity was less than or equal to 10% of the phosphomonoesterase activity (for pNPhP) as evidenced by the lack of hydrolysis of bis(p-nitrophenyl)-phosphate and cyclic 3',5'-AMP. The ability of these substances to inhibit hydrolysis of pNPhP reflected their capacity as substrates, i.e. the most inhibitory were the most rapidly hydrolyzed.
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PMID:Calf thymus alkaline phosphatase. I. Properties of the membrane-bound enzyme. 1 42

Responses of Rhizoctonia solani to herbicides in soil cultures were assessed by measuring soil enzyme activity and other growth-related factors. Both beta-galactosidase (EC 3.2.1.23) and phosphatase (EC 3.1.3.1.3.1.3.2) activities were highly correlated with amounts of mycelium in soil. Both enzyme activities were reduced significantly by either fluometuron or prometryn at 40 microgram/g of soil; the pathogen was more distinctly suppressed by fluometron and showed a stronger tendency to overcome the effects of prometryn with time. Inhibition was also reflected in reduced ultilization of glucose and less CO2-C evolved. Except for an increase in beta-galactosidase activity in the presence of 1 microgram fluometuron, low levels of either herbicide had little effect on the pathogen.
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PMID:Effects of the herbicides fluometuron and prometryn of Rhizoctonia solani in soil cultures. 1 60

Membrane-bound alkaline phosphatase of Bacillus licheniformis 749/c is derepressed by glucose in complex and chemically defined media. In the presence of lactate, pyruvate, or succinate the synthesis is repressed. The lactate repression neither affects total protein synthesis nor inhibits penicillinase synthesis. Thus, carbon sources specifically influence alkaline phosphatase synthesis. Although variations in the inorganic phosphate content of the growth media directly affect alkaline phosphatase synthesis, the intracellular inorganic and total phosphate pools appear to be unrelated to its repression or derepression. During lactate repression there is preferential incorporation of lactate molecules into glycogen, whereas no such incorporation could be detected from glucose. Net glycogen synthesis remains the same in glucose- or lactate-grown cells. It is postulated that, in phosphate-deficient growth medium, gluconeogenic metabolism regulates alkaline phosphatase synthesis.
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PMID:Interrelationship of carbohydrate metabolism and alkaline phosphatase synthesis in Bacillus licheniformis 749/c. 1 80

Changes in ECG, free calcium (CaF), and other biochemical parameters were measured during reinfusion of citrate anticoagulated blood in 12 subjects undergoing plateletpheresis. Physical symptoms during the procedure were also monitored. The CaF was found to correlate best with the Q-oTc interval as compared to the Q-oT, Q-Tc, or Q-T interval. While the correlation was significant (r = 0.592, p less than .001), the Q-oTc could not predict the CaF. A number of other blood constituents were found to change during plateletpheresis, with most directly related to either citrate administration or hemodilution. Severe physical symptoms were found in one subject and no symptoms in three. In the subjects without symptoms the changes in Q-oTc, Pi, alkaline phosphatase, and glucose through the plateletpheresis procedure were different from changes in all subjects. The decrease in glucose level was the most striking single factor correlating with the lack of physical symptoms during the citrate-induced hypocalcemia associated with plateletpheresis. It is concluded that monitoring of the ECG cannot substitute for direct measurement of free calcium in citrate-induced hypocalcemia, that the physical symptoms associated with similar levels of hypocalcemia are variable, that glucose level may be a marker for the effects of citrate-induced hypocalcemia, and that lowered citrate loads during plateletpheresis appear warranted.
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PMID:Relationship of physical symptoms, ECG, free calcium, and other blood chemistries in reinfusion with citrated blood. 3 18

Individual heritability and differences in the concentration of the chemical components of the blood were studied in the dairy cows of the Slovak Spotted breed. The experiment was performed with 166 cows. The set comprised six groups of half-sisters from three stocks. The differences among the cows were statistically significant (alpha = 0.01) in the majority of the parameters studied: haematocrit, haemoglobin, pH, PO2, oxygen saturation of the blood; plasma potassium, phosphorus, magnesium, calcium, total protein, urea, glucose, alkaline phosphatase, and esterified fatty acids. The coefficients of repeatibility for the mentioned parameters ranged from 0.19 to 0.75. The heritability coefficients were calculated for the parameters in which the inter-group differences were significant: total protein (0.62), magnesium (0.57), potassium (0.51), urea (0.49), glucose (0.45), phosphorus (0.43), calcium (0.39), haematocrit (0.37), haemoglobin (0.35), pO2 (0.29). The results suggest that some of the parameters under study are under certain genetic control.
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PMID:[Genetically conditioned variability of metabolic profile parameters in dairy cows]. 3 53

Twelve metabolically healthy patients, who had to undergo cholecystectomy or gastric resection, were fed intermittently by the parenteral route (via veins of the upper limbs) post-operatively up to and including the 2nd post-operative day with a combined maltose-glucose solution in parallel with an 8% mixture of crystalline L-aminoacids. At an administration rate of 150 g maltose/day and 250 g glucose/day with the simultaneous administration of 80 g aminoacids, the mean carbohydrate utilisation was 82,5%. The glucose and maltose levels in the blood fluctuated in accordance with the infusion periods and the free fatty acids levels measured were their mirror image. On the whole free fatty acids were lowered significantly, which indicates adequate carbohydrate supply with consequent inhibition of lipolysis. The degree of tolerance was determined objectively by measurement of the acid-base parameter, gamma-GT, alkaline phosphatase, GOT, bilirubin, uric acid, creatinine and serum electrolytes. No changes were found which could be attributed to the administration of the infusion solution.
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PMID:[Utilization of maltose during shorttime parenteral nutrition (author's transl)]. 4 94

Intact Angiostrongylus cantonensis is able to hydrolyse glucose-phosphate esters, mononucleotides and rho-nitrophenyl phosphate as well as beta-glycerophosphate in vitro. Reciprocal inhibition studies suggest that the hydrolysis of such substrates is due to a non-specific phosphomonoesterase. Molybdate ions, which exert no effect on either the uptake of glucose or the production of lactate, inhibit the hydrolysis of glucose-1-phosphate in the external medium and simultaneously lower the production of lactate by the intact worms in vitro.
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PMID:Acid phosphatase activity demonstrated by intact Angiostrongylus cantonesis with special reference to its function. 4 61

5'-Nucleotidase, assayed as 5'-AMPase, has been extensively characterized and established as a stable, quantitative plasma membrane marker in HeLa S3 cells. The membrane 5'-AMPase has a Km of 7.0 microM. Relative affinities of the other 5'-mononucleotides for the enzyme are 5'-GMP > 5'-TMP > 5'-UMP > 5'-CMP. There are activity optima at pH7 and 10; the latter is Mg(2+)-dependent. The membrane preparations have a small amount of acid phosphatase activity that is distinct from 5'-AMPase activity but no alkaline phosphatase. AOPCP, ADP, and ATP are strongly inhibitory. Mg2+, Ca2+, or Co2+ additions do not affect the pH 7.0 activity; Mn2+ activates slightly, whereas Zn2+, Cu2+, and Ni2+ are inhibitory. EDTA slowly inactivates, but removal of the EDTA without the addition of divalent cations restores activity. The inactivation is also substantially reversed by Co2+ or Mn2+, but reactivability by divalent cations decreases with time in EDTA. ConA strongly inhibits, and alpha-methyl-D-mannoside or glucose (the latter much less efficiently) relieves the inhibition, indicating that the 5'-AMPase is a glycoprotein. Histidine is also inhibitory. Ouabain, phloretin, cytochalasin B, cysteine, phenyl-alanine, MalNEt, and IAA are without effect. 5'-AMPase activity codistributes with pulse-bound [3H]ouabain when either of two cell fractionation procedures are used. The 5'-AMPase activity per cell is constant at different cell densities in exponentially growing cells, and activity per unit cell volume remains constant throughout the cell cycle. These properties, together with its absence in other organelles, its stability to storage, its insensitivity to certain experimental manipulations, and its general insensitivity to inhibitors of specific transport systems, make 5'-AMPase a useful quantitative marker in studies on the regulation of HeLa membrane transport systems. Key Words: HeLa, 5'-nucleotidase, plasma membrane marker, non-specific phosphatases, divalent ions, ConA, AOPCP, cell cycle, mitochondria, transport inhibitors.
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PMID:Characterization of HeLa 5'-nucleotidase: a stable plasma membrane marker. 4 80

Synovial fluid and blood were collected from 18 clinically healthy brood mares in resting conidition. The following parameters were analysed: total leucocytes, glucose, alkaline phosphatase (AP), lactate dehydrogenase (LDH), total protein, albumin, total globulin, albumin/globulin ratio and electrophoretic protein picture. The serum/synovia ratios were calculated for all parameters. It was considered to be of greater diagnostic value to compare these serum/synovia ratios rather than to look at the individual concentrations in synovia. The results obtained did not materially differ from those in the existing literature. In addition, this study confirmed that small protein molecules could more easily penetrate the synovial membrane than high-molecular proteins.
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PMID:Studies on the synovia in healthy horses with particular reference to the protein composition. 6 47


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