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)

We treated 60 patients with blunt liver injury over 14 years. According to Makiya's scale of severity, 22 of these lesions (37%) were of Type I, 23 (38%) of Type II, and 15 (25%) of Type III. The overall mortality rate was 23% (14 patients). Changes in hepatic function were studied in these patients. Transaminase levels showed abnormal elevations immediately after the injury but rapidly decreased to normal levels within about 40 days in both the patients who survived the injury and those who died. The alkaline phosphatase activity showed moderate gradual elevations with time, exceeding 20 K.A. units 10 days after the injury in those who died. The total bilirubin level increased to only about 4 mg/dl in those who survived but exceeded 8 mg/dl 10 days after the injury in about 80% of those who died. The total cholesterol level decreased below 100 mg/dl in those who died. In chloric cobalt reaction, the R-value shifted to the left in those who survived but to the right in those who died. Total plasma protein, which decreased to about 6.0 gm/dl immediately after the injury, gradually recovered in those who survived but further declined in those who died. Percentage of gamma-globulin increased but remained below 20% in those who survived but exceeded 20% within 10 days of injury in many of those who died. Hepatic functions 5 years after the injury were generally within the normal range.
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PMID:Short-term and long-term changes in hepatic function in 60 patients with blunt liver injury. 243 2

We describe a new method for light microscopic demonstration of alkaline phosphatase (ALP) activity in plastic-embedded sections. Rat tissues were fixed in acetone (-20 degrees C), infiltrated in glycol methacrylate (GMA), and embedded at 0 degrees C. Sections were cut at 1 and 2 microns, dried at room temperature, and incubated in the conventional Gomori medium. Cerium chloride was used to convert calcium phosphate into cerium phosphate, which was subsequently converted into cerium perhydroxide. The slight yellow precipitate of cerium perhydroxide was amplified using 3,3'-diaminobenzidine tetrahydrochloride (DAB). For comparison, tissue sections were processed according to the calcium-cobalt method. The method described combines exact localization of ALP activity with optimal preservation of tissue morphology.
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PMID:Enzyme histochemical demonstration of alkaline phosphatase activity in plastic-embedded tissues using a Gomori-based cerium-DAB technique. 246 38

Hexammine cobalt(III) chloride (Co(NH3)6(3+) provokes a B-DNA----Z-DNA----psi-DNA conformational transition in poly(dG-dC).poly(dG-dC) and poly(dG-m5dC).poly(dG-m5dC). The circular dichroism spectrum of psi-DNA is characterized by a manyfold increase of positive ellipticity in the range of 300-225 nm and the complete absence of a negative peak. In order to ascertain the helical handedness of psi-DNA, we used a recently developed enzyme immunoassay technique. This method consisted of treating the polynucleotides with Co(NH3)6(3+) to convert them to the Z- or psi-DNA forms and immobilizing these conformations on a microtiter plate. The plates were subsequently treated with a monoclonal anti-Z-DNA antibody Z22, alkaline phosphatase conjugated, affinity purified immunoglobulins, and the phosphatase substrate. The enzyme-substrate reaction was monitored by reading the absorbance at 405 nm with a microplate autoreader. The monoclonal anti-Z-DNA antibody had no reactivity to the B-DNA form, but bound strongly to both the Z- and psi-DNA forms, showing that Co(NH3)6(3+)-induced psi-DNA form of the polynucleotides exists in the left-handed Z-DNA conformation.
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PMID:Direct evidence for the presence of left-handed conformation in a supramolecular assembly of polynucleotides. 266 Jan 2

An enzyme with FAD pyrophosphatase activity was extracted from human placental syncytiotrophoblast microvilli and purified to near-homogeneity. The enzyme has been identified as 5'-nucleotidase by several criteria. Throughout purification, parallel increases in the specific activities of FAD pyrophosphatase and AMP phosphatase were observed. The enzyme was a glycoprotein with a subunit molecular weight of 74,000. EDTA treatment resulted in a marked decline in both activities, and restoration of FAD pyrophosphatase activity but not 5'-nucleotidase activity was accomplished by the addition of Co2+ or, to a lesser extent, Mn2+. The substrate specificity of the 5'-nucleotidase activity that we observed agreed closely with the results of others. The pyrophosphatase activity was relatively specific for FAD. ADP, ATP, NAD(H), and FMN were not hydrolyzed, and ADP strongly inhibited both activities. For FAD pyrophosphatase activity, a Km of 1.2 x 10(-5) M and a Vmax of 1.1 mumol/min/mg protein were determined in assays performed in the presence of Co2+. In the absence of added Co2+, the Vmax declined but the Km was unchanged. For 5'-nucleotidase (AMP as substrate) the Km was 4.1 x 10(-5) M and the Vmax 109 mumol/min/mg protein. Hydrolysis of FMN to riboflavin was observed in partially purified detergent extracts of microvilli that contained alkaline phosphatase activity and lacked FAD pyrophosphatase and 5'-nucleotidase activity. The presence of both FAD pyrophosphatase and FMN phosphatase activities in syncytiotrophoblast microvilli supports the view that the placental uptake of vitamin B2 involves the hydrolysis of FAD and FMN to riboflavin which is then absorbed, a sequence postulated for intestinal absorption and liver uptake.
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PMID:5'-Nucleotidase of human placental trophoblastic microvilli possesses cobalt-stimulated FAD pyrophosphatase activity. 284 89

Although WR-2721, S-2-(3-aminopropylamino)ethylphosphorothioic acid, is an effective radioprotector, its use is limited by its toxicity. Combining WR-2721 with other agents might decrease its toxicity and/or increase its effectiveness. The effect of selenium (Se) pretreatment on the acute toxicity and radioprotective effect of WR-2721 was studied in male CD2F1 mice. Injection of 1.6 mg/kg Se 24 hr before WR-2721 (800-1200 mg/kg, IP) decreased the lethality of WR-2721 significantly. Lower doses of Se were also effective, but simultaneous administration was not effective. Se injection alone (1.6 mg/kg) 24 hr before cobalt-60 irradiation increased the survival (dose reduction factor, DRF = 1.1) significantly. A synergistic effect on post-irradiation survival was observed when Se was injected 24 hr before WR-2721 (200-600 mg/kg IP 1/2 before irradiation). For example, after exposure to 22 Gy (1 Gy/min), 30-day survival was 100% when mice were treated with both Se and 600 mg/kg WR-2721, and was 13% with WR-2721 alone. The DRF after 400 mg/kg WR-2721 was 2.6 with Se compared to 2.2 without Se pretreatment. Alkaline phosphatase activity in bone marrow cells and serum was significantly depressed after treatment with 1.6 mg/kg Se, suggesting that a retardation of conversion of WR-2721 to its active free sulfhydryl form through the action of alkaline phosphatase might be partly responsible for the effects of Se. Other possible mechanisms related to the antioxidant properties of Se are under investigation.
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PMID:Selenium pretreatment enhances the radioprotective effect and reduces the lethal toxicity of WR-2721. 285 28

Activity of cobalt activated acylase, gamma-glutamyltransferase, leucylaminopeptidase and alanylaminopeptidase in serum and liver of mice with transplantable leukemias (L1210, L1210/ara-C, L1210/CH3-G, AKSL-4, plasmacytoma ADJ-PC-5) were determined. Adenosinotriphosphatase, 5'-nucleotidase and alkaline phosphatase were histochemically localized in lymphatic nodes and spleen. Among the investigated enzymes the rise in serum activity of cobalt activated acylase and gamma-glutamyltransferase was demonstrated. A substantial increase of leucylaminopeptidase and alanylaminopeptidase was shown in the liver. A decrease in the histochemical reactions of all the studied enzymes was observed.
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PMID:Enzyme activity in mice with transplantable leukemia. 287 46

The electronic and 1H NMR spectra are reported for the cobalt(II) alkaline phosphatase (EC 3.1.3.1.) system at pH around 6 in the range 0-2 mol of cobalt per mol protein. It is shown that under the present experimental conditions cobalt(II) selectively populates the A sites. Three isotropically shifted NH signals have been detected in the A site that indicate the presence of three histidines in the coordination sphere of cobalt(II). The electronic spectra and the nuclear relaxation properties are consistent with pentacoordination of cobalt(II) in the A site. The finding of reproducible preparation routes for the derivatives, and of appropriate experimental conditions for the observation of their 1H NMR spectra, open new possibilities for the spectroscopic investigation of alkaline phosphatase.
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PMID:A spectroscopic investigation of cobalt(II) substituted alkaline phosphatase. 329 44

The effect of essential trace metals on bone metabolism was investigated in the femoral diaphysis of weanling rats. Oral administration of zinc (1.53-306 mumol/100 g body weight) for 3 days produced significant increases in alkaline phosphatase activity and DNA content. These biochemical indices were also increased by oral administration of chromium (III), cobalt, copper, manganese, and nickel with the dose of 1.53 mumol/100 g. With the dose of 15.3 mumol/100 g of above all metals, except zinc, the enzyme activity was significantly decreased in comparison with control, while DNA content was not decreased significantly. Moreover, the effect of zinc on alkaline phosphatase activity and DNA content was not enhanced by simultaneous administration of other metals (1.53 mumol/100 g). The present study indicates that, of the essential trace metals, zinc can effectively stimulate the bone growth and calcification with comparatively higher dose levels. This suggests a nutritional significance of zinc on bone growth.
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PMID:Effect of essential trace metals on bone metabolism in weanling rats: comparison with zinc and other metals' actions. 379 21

The effects of zinc on the enzymes of femoral tissue were investigated in weanling rats that had been given zinc sulfate (1.0 mg Zn2+/100 g body wt) p.o. for 3 days. Administration of zinc caused a marked elevation of alkaline phosphatase and acid phosphatase activities, whereas it did not cause significant changes in succinate dehydrogenase, 5'-nucleotidase, ATPase, pyrophosphatase and beta-N-acetylglucosaminidase activities. The effect of zinc was greater on alkaline phosphatase of the femoral diaphysis. Zinc content of the femoral diaphysis was raised significantly by administration of zinc. The addition of zinc in concentrations of 10(-2)-10(2) microM did not produce a significant increase in alkaline phosphatase activity in the femoral diaphysis, indicating that zinc could not activate the enzyme. Administration of cycloheximide or actinomycin D completely inhibited the increase in alkaline phosphatase activity produced by administration of zinc. DNA content of the femoral diaphysis, but not epiphysis, was increased markedly by administration of zinc. The increases in both alkaline phosphatase activity and DNA content of the femoral diaphysis were not caused by administration of copper, manganese, cobalt, nickel and chromium(III). The present investigation suggests that zinc may induce the increase in alkaline phosphatase related to DNA synthesis and, as a result, stimulate bone growth.
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PMID:Action of zinc on bone metabolism in rats. Increases in alkaline phosphatase activity and DNA content. 395 86

Some properties of inorganic pyrophosphatase (PPiase EC 3.6.1.1.) and para-nitrophenylphosphatase (p-NPPase EC 3.1.3.1) in the microsomal fraction of odontoblasts were investigated. The ratio of Mg2+:p-NPP and Mg2+:PPi for optimal enzyme activities was 1:1. A mutual substrate competition for PPiase and p-NPPase was described. In the presence of 0.1 mM EDTA, Mg2+ alone was not able to reactivate p-NPPase or PPiase. Instead, Zn2+ and Co2+ reactivated the PPiase, indicating they might act as cofactors for the enzyme. Mg2+ increased the PPiase activity, probably because Mg PP2-i was the true substrate for the enzyme. The diphosphonates ethane-1-hydroxy 1,1 diphosphonate (EHDP), methane diphosphonate (MDP) and dichloromethane diphosphonate (Cl2MDP) inhibited the PPiase activity.
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PMID:Relationship of inorganic pyrophosphatase and para-nitrophenylphosphatase activities of alkaline phosphatase in the microsomal fraction of isolated odontoblasts. 612 84


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