Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Fractionation of serum alkaline phosphatase by either biochemical or electrophoretic techniques is often insufficient to determine the source of the elevated serum enzyme. In 31 unselected patients with high serum alkaline phosphatase a simultaneous determination of serum gamma glutamyl transpeptidase and urinary hydroxyproline excretion rates was performed, in addition to urea denaturation and L-phenylalanine inhibition tests. Of 25 patients with definite diagnosis, the urea denaturation test correctly identified the source of the elevated serum alkaline phosphatase (ALP) in 16 (64 percent). The serum gamma-glutamyl transpeptidase (GGTP) alone predicted the correct diagnosis in 64 percent of the cases and the urinary hydroxyproline (HOP) alone in 69 percent. When all three tests were performed simultaneously, the combination of results identified the source of the ALP in 88 percent of the cases. It is believed that this combination offers better sensitivity and specificity than any of the three tests used individually.
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PMID:A supplement to alkaline phosphatase fractionations: utilization of gamma-glutamyl transpeptidase and hydroxyproline assays. 2 40

A membrane-bound insoluble alkaline phosphatase (APase) and an extracellular soluble APase were purified, respectively, from a membrane preparation of Bacillus subtilis 6160-BC6, which carries a mutation to produce APase constitutively, and from a culture fluid of a mutant strain. RAN 1, isolated from strain 6160-BC6, which produces an extracellular soluble APase. The two preparations were homogeneous, as judged by sodium dodecyl sulfate discontinuous gel electrophoresis and by gel electrophoreses in the presence of 8 M urea at pH 9.3 and 4.3. RAN 1 APase was crystallized. Both preparations possessed phosphatase and phosphodiesterase activities, and their pH optima were both at 9.5. They were competitively inhibited by phosphate or arsenate and were activated by the addition of Ca2+ but not by Zn2+. The APase and alkaline phosphodiesterase activities seemed to be contained in the same protein molecule. The molecular weight of 6160-BC6 APase was estimated to be 46,000 +/- 1,000, and that of RAN 1 APase was estimated to be 45,000 +/- 1,000. The largest difference between the 6160-BC6 and RAN 1 APase's was in solubility in low-ionic-strength solutions. Present results suggest that each enzyme is composed of a single polypeptide chain and that 6160-BC6 APase aggregates in solutions of low ionic strength.
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PMID:Purification and characterization of extracellular soluble and membrane-bound insoluble alkaline phosphatases possessing phosphodiesterase activities in Bacillus subtilis. 2 78

Alkaline phosphatase was purified from plasma membranes of rat ascites hepatoma AH-130, the homogenate of which had 50-fold higher specific activity than that found in the liver homogenate. The presence of Triton X-100, 0.5%, was essential to avoid its aggregation and to stabilize its activity. The purified enzyme, a glycoprotien, was homogeneous in polyacrylamide gel electrophoresis. Polyacrylamide gel electrophoresis in sodium dodecyl sulfate indicated a protein molecular weight of 140,000. The addition of beta-mercaptoethanol caused the dissociation of the alkaline phosphatase into two subunits of identical molecular weight, 72,000. Isoelectric focusing revealed that the pI of this enzyme is 4.7. The pH optimum for the purified enzyme was 10.5 or higher with p-nitrophenylphosphate, and slightly lower pH values (pH 9.5--10.2) were obtained when other substrates were used. Of the substrates tested, p-nitrophenylphosphate (Km-0.3 mM) was most rapidly hydrolyzed. Vmax values of other substrates relative to that of p-nitrophenylphosphate were as follows; beta-glycerophosphate, 76%; 5'-TMP, 82%; 5'-AMP, 62%; 5'-IMP, 43%; glucose-6-phosphate, 39%; ADP, 36% and ATP, 15%. More than 90% of the activity of the purified enzyme was irreversibly lost when it was heated at 55 degrees C for 30 min, or exposed either to 10 mM beta-mercaptoethanol for 10 min to 3 M urea for 30 min, or to an acidic pH below pH 5.0 for 2 h. Of the effects by divalent cations, Mg2+ activated the enzyme by 20% whereas Zn2+ strongly inhibited it by 95% at 0.5 mM. EDTA at higher than 1 mM inactivated the enzyme irreversibly, although the effect of EDTA at lower than 0.1 mM was reversible by the addition of divalent cations, particularly by Mg2+. The enzyme was most strongly inhibited by L-histidine among the amino acids tested, and also strongly inhibited by imidazole. These results suggest that alkaline phosphatase of rat hepatoma AH-130 is very similar to that of rat liver in most of the properties reported so far.
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PMID:Purification and characterization of alkaline phosphatase from plasma membranes of rat ascites hepatoma. 2 78

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

The present study reports of three kinds of experiments of unaffected primary rejection of xenogenous kidney transplanats in the close-related fox-dog species system. The issue is whether there is a relation between the amount of grafted parenchyma and the immune induced potency, that is whether the course of rejection of transplanted single kidneys (group I a) differs from the course after en-bloc transplantation of both kidneys (group I b). In group II alterations of blood chemism and behavior of humoral antibodies are followed in dogs to which a fox kidney was transplanted, while keeping their own functioning kidneys. This experiment is to give information whether the uremic syndrome influences the development of humoral immunity, and what changes of blood chemism may primarily be related to destruction of the graft, under the condition of absent uremia. Untreated graft recipients survived for 5,4 +/- 0,49 days (n = 5) when single kidneys were transplanted (group I a), and 5,2 +/- 0,75 days (n = 5) when both kidneys were grafted en-bloc (group I b). As to the rejecting reactions, both groups are almost equal: the increasing functional failure causes a fast increase of creatinine and urea nitrogen; alkaline phosphatase and LDH show distinct alterations, related to the progress of the graft's destruction. Decrease of albumin level and loss of cholinesterase activity indicate an impaired hepatic function as reaction to uremic intoxication. Gamma-globulins and leucocytes show alterations that can be related to non-specific inflammatory reactions. The immunologically specific initial lymphopenia suggests that after revascularization these cells migrate to the graft, and later react with antigenic structures of vascular endothelium and still later with those of the organ cells. Cytotoxic antibodies appear on the 4th postoperative day in increasing amount. Post mortem histologic examination shows round cell infiltrates in the vastly necrotic renal parenchyma. When the recipient's kidneys are kept in situ and a fox kidney is transplanted (group II) uremia is avoided and the animals survive. During the 30-days period of observation, that is longer than the term of rejection, the titer of cytotoxic antibodies remains stable or tends to increase. LDH and alkaline phosphatase show characteristic changes that are considered sequels from destructed transplantate. The experiments show, aside from certain reservations, that the donor-host combination fox-dog is suitable to serve as preclinic model for human transplantation using xenogenous donors of organs, i. e. anthropoid primates.
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PMID:[The unaffected primary rejection of xenogeneic kidney transplants in the closely related fox-dog species system]. 3 59

In a 24-hour study, plasma peak lithium was determined in manic-melancholic patients who routinely had their entire lithium dose at night. A correlation analysis was undertaken of the relation of plasma peak level and the dose of lithium to a number of lithium induced changes: Increase in urine volume, weight gain, decrease in plasm phosphate, increase in plasma magnesium, decrease in plasma urea, increase in plasma alkaline phosphatase, increase in urinary pH. Only the changes in plasma phosphate and in urine pH were significantly correlated to the peak value of plasma lithium. The increase in urine volume was significantly correlated to the dose of lithium.
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PMID:Lithium effects: relation to lithium dose and to plasma peak levels. 4 12

The following blood indices were determined in the blood of 34 pregnant sows of the Large White breed under standard feeding conditions: haemoglobin, haematocrit, leucocytes, and--in the blood serum, --total protein, glucose, urea, bilirubin, cholesterol, enzyme activity (AP, GOT, GPT, GGTP) and mineral concentrations (Ca, P--inorg., Mg, Na, K, Fe, Cu, Zn, Mn). The blood was sampled in the first and third pregnancy at an average live weight of 165.12 and 197.36 kg, at an average age of 318 and 630 days and at an about the same average length of pregnancy in the time of both samplings (59 days). In younger, still growing gilts (first pregnancy) a significantly (P less than 0.05) lower content of total protein, magnesium, iron and copper was revealed, as compared with adult sows. The content of glucose, calcium, potassium and manganese in the blood serum of the gilts was significantly (P less than 0.05) higher than in sows in their third pregnancy. The adult sows showed a significantly (P less than 0.05) lowered activity of alkaline phosphatase and gamma-glutamyl transpeptidase, as distinct from gilts.
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PMID:[The effect of pregnancy order on various biochemical and hematological values in sows]. 10 42

Sera from 129 squirrel monkeys, Saimiri sciureus, were analyzed for 15 chemical constituents. The values obtained were then analyzed for statistical significance causing the following sets of variables: (1) colony-bred versus noncolony-bred, (2) karyotype (3) vendor, (4) sex and (5) dietary iodine supplementation versus nonsupplementation. Calcium, inorganic phosphorous, albumin, uric acid, blood urea nitrogen, glucose, alkaline phosphatase and potassium were high in colony-bred animals. Cholesterol, total protein and chloride were lower in colony-bred animals than in noncolony-bred animals. No differences were seen in total bilirubin, lactic dehydrogenase, serum glutamic oxaloacetic transaminase and sodium. When the noncolony-bred animals were separated by karyotype, total protein was higher and chloride was lower between animals from Peru versus from Guyana. Colombian animals had total protein values lower than Peruvian and lactic dehydrogenase values higher than Peruvian. Colony-bred Peruvian monkeys had serum glutamic oxaloacetic transaminase values higher than colony-bred Colombian monkeys. No differences were observed between monkeys from different vendors. Chemical constituents higher between noncolony-bred males and females were calcium and alkaline phosphatase. There were no differences observed for colony-bred males and females. Dietary iodine supplementation appeared to increase both total bilirubin and calcium.
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PMID:Baseline blood chemistry determinations in the squirrel monkey (SAimiri sciureus). 11 Sep 77

Normal values for a number of blood components of grivet monkeys are reported. Haematological data and values for glucose, cholesterol and urea are similar to those of rhesus monkeys. Activities of alkaline phosphatase (1526 U/l), glutamine oxaloacetate transaminase (30.9 U/l), glutamine pyruvate transaminase (13.7 U/l), lactate dehydrogenase (629 U/l), alpha-hydroxybutyrate dehydrogenase (175 U/l), creatine phosphokinase (227 U/l), gamma-glutamyl transpeptidase (38.7 U/l) and sorbitol dehydrogenase (14.2 U/l), and levels of lysozyme (178 mg/dl), zinc (162 microgram/dl), copper (81.3 microgram/dl) and iron (296.5 microgram/dl) have not previously been reported for this animal. Values for serum amino acids, proteins, electrolytes, triglycerides and creatinine are compared with those of other primates.
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PMID:Normal values for some whole blood and serum components of grivet monkeys (Cercopithecus aethiops). 11 24

Another Kasahara-variant alkaline phosphatase isoenzyme was found in 2 out of 25 human renal cell carcinoma tissues. This enzyme electrophoresed in a single diffuse band which is cathodal to but continuous with the liver alkaline phosphatase. After neuraminidase treatment, this enzyme electrophoresed in the same position as that of neuraminidase-treated Kasahara isoenzyme. The enzymic properties of another neuraminidase-treated Kasahara-variant enzyme such as inhibitions by L-phenylalanine, L-homoarginine, L-tryptophan, and L-leucine, effects of inorganic phosphate, urea, and sodium dodecyl sulfate, heat stability, and the reactivity with concanavalin-A are consistent with those of Kasahara isoenzyme. On Ouchterlony's double diffusion, the precipitin lines of Kasahara and the new variant enzyme produced by antibody to Kasahara isoenzyme fused completely. These facts may indicate the occurrence of another Kasahara-variant isoenzyme.
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PMID:Another Kasahara-variant alkaline phosphatase in renal cell carcinomas. 11 99


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