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)

Polyacrylamide gel electrophoresis of sera obtained from normal individuals shows an incidence (33%) of double and triple bands of alkaline phosphatase in the beta-lipoprotein zone in addition to the usual ones near beta-globulin. The correlation between the occurrence of a slow moving band in addition to the normal one, of different intensities, p+ and p++ with O and B groups has been further confirmed. No relationship was observed between the width or the number of bands with the total amount of alkaline prosphatase as determined biochemically.
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PMID:Electrophoretic variants of alkaline phosphatase in normal human populations. 103 Aug 30

Procedures developed for in vitro pellicle formation in intact enamel proved useful for relating qualitiative characteristics of dental pellicle to a number of factors. Coronal surfaces of extracted human molars from experimental and control groups were pumiced, sterilized, and incubated for two hours at 37 C in parotid saliva and distilled water, respectively. Pellicle proteins were desorbed sequentially with water and 0.2 M sodium phosphate, with a pH of 7.0. Polyacrylamide disc electrophoresis of the desorbates yielded distinct patterns, indicating selective adsorption of proteins from saliva, varying affinity to enamel, and the presence of proteins not acquired in vitro from saliva. Certain pellicle components, including amylase and IgA, showed a relatively weak affinity for enamel and were eluted in part by water; other proteins were desorbed only by phosphate buffer. Anionic electropherograms of the phosphate desorbates showed an increase in the two most anodic proteins relative to corresponding salivary bands. An intense anodic protein and two minor bands were eluted by water or buffer from the surface of control as well as experimental teeth but not from teeth coated with sealants. Serum albumin and alkaline phosphatase were identified as components of the extra-salivary material. Further investigation of the sources and functions of the constituents of the protein layer generally considered as "acquired" dental pellicle appears warranted.
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PMID:Characteristics of an in vitro dental pellicle. 106 Jun 64

Polyacrylamide gel electrophoresis (PAGE) of alkaline phosphatase (AP) was performed in 116 patients with elevated AP and in 36 controls. Results were compared with clinical data and with the heat inactivation techniques for AP isoenzyme separation. This latter method is simple but approximate; it is without value in the case of coexistent bone and liver pathology. PAGE gave a clear separation of liver, bile, bone, and intestinal AP isoenzymes. Disagreement with clinical data was rare (6 out of 86) and occurred in cases of associated bone and liver pathology (with 1 exception only), where one of these two abnormalities was not detected. Heat inactivation is useful as a screening test. If the cause of the elevated AP remains unknown after a few simple examinations, PAGE should then be utilized. Although more time-consuming, it is certainly more effective in the separation of AP isoenzymes.
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PMID:[Alkaline phosphatase isoenzymes. Selection of the seperation methods and their diagnostic value]. 115 82

A transplantable ascites-forming osteosarcoma (J. H. 1-AOS) derived from the 35th generation of spontaneous osteosarcoma, J. H. 1-OS, grown in Fischer 344 syngeneic rats was established. Tumorigenicity, histochemical and ultrastructural characteristics were investigated. Rats carrying the ascites form osteosarcoma died of cachexia about 15 days after transplantation, 1.5-2.5 x 10(6) cells/ml of tumor cells generally being involved in the ascites and tumor nodules formed in the mesentery. After inoculation into the back subcutaneous space, tumor growth was very rapid. Small round cells were detected in the Giemsa stain smear, and although osteoid formation was histologically lacking, cell surface alkaline phosphatase activity was noted both light and electron microscopically. Polyacrylamide gel electrophoresis demonstrated that alkaline phosphatase (Al-p) extracted from this tumor was consistent with Al-p from rat fetal calvaria. Thus maintenance of osteogenic potential is suggested for these ascites osteosarcoma cells, indicating their usefulness for further studies of biological behaviors of this tumor type.
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PMID:[Establishment and characterization of an ascites-forming rat osteosarcoma cell line]. 154 42

Polyacrylamide gel electrophoresis utilizing sodium dodecyl sulfate followed by specific staining for alkaline phosphatase was accomplished using sera from patients with osteosarcoma, polyostotic fibrous dysplasia, metastatic bone tumor, and idiopathic hyper-alkalinephosphatasemia. Alkaline phosphatase activity of the sera was uniformly demonstrated at a molecular weight of 60,000. L-homoarginine more strongly inhibited the alkaline phosphatase activity than did L-phenylalanine. Alkaline phosphatase activity was markedly inactivated by heating. Regarding substrate specificity, the hydrolysis of p-nitro-phenylphosphate occurred at a lower rate than did that of phenylphosphate. By contrast, the hydrolysis of alpha- and beta-glycerophosphate occurred at a higher rate than did that of phenylphosphate. As seen from the data presented here, the serum alkaline phosphatase samples obtained from these patients with skeletal disorders have several common characteristics.
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PMID:[Identification of serum alkaline phosphatase from human bone]. 169 Jul 86

Oligomycin-sensitive particulate ATPase (MB ATPase) from L. donovani promastigotes was solubilized by chloroform treatment. Polyacrylamide gel electrophoresis revealed several protein bands, with the major one possessing ATPase activity. The solubilized enzyme had Mg2+-ATPase and Ca2+-ATPase but no K+-dependent alkaline phosphatase activity. The Mg2+-ATPase activity was stimulated by monovalent cations and was not sensitive to oligomycin. Hence it is referred to as F1 ATPase. It had optimum activity at pH 7.6 and 30 degrees C. The Arrhenius plot for MB ATPase was biphasic with activation energies (Ea) of 16.2 and 3.4 kcal mol-1, while F1 ATPase exhibited a linear plot with Ea = 10.1 kcal mol-1. Lineweaver-Burk plots were biphasic with Km values of 0.17 and 1.25 mM for MB ATPase and 0.18 and 1.33 mM for F1 ATPase. The enzyme could be preserved at -15 degrees C in Tris-SO2-(4)-EDTA-ATP-glycerol (t1/2 = 20 days).
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PMID:Solubilization and kinetic characterization of mitochondrial adenosine triphosphatase from Leishmania donovani promastigotes. 297 May 89

Polyacrylamide gel electrophoresis of alkaline phosphatase may yield abnormally migrating fractions; these include high-molecular-mass alkaline phosphatase, which remains at the gel origin, and immunoglobulin-alkaline phosphatase complexes, which have a mobility approximately 1/3 that of liver isoenzyme. We performed a retrospective study of 19 patients whose sera exhibited atypical alkaline phosphatase fractions, defined as bands whose mobility was slower than bone, liver, or intestinal alkaline phosphatase; 17 had a mobility approximately 1/3 that of liver isoenzyme and 16 also exhibited gel origin enzyme activity or high-molecular-mass bands. The strong association of the atypical and high-molecular-mass alkaline phosphatases suggests that they may be structurally related, both consisting of either immunoglobulin-enzyme complexes or membrane-alkaline phosphatase complexes. This hypothesis is supported by (1) one serum available for investigation containing alkaline phosphatase-immunoglobulin complexes in both abnormally migrating fractions, but on detergent treatment showing no evidence of membrane-bound enzyme; (2) detergent treatment of serum from patients with only high-molecular-mass alkaline phosphatase creating bands with a mobility of approximately 1/3 that of the liver isoenzyme.
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PMID:Association of high-molecular-mass and electrophoretically atypical alkaline phosphatases. 312 Dec 11

This paper is an attempt to the analysis of the main biochemical characteristics of alkaline phosphatase from sheep polymorphonuclear neutrophils. Ten male adult Romanoff X Berrichon sheep were studied. Alkaline phosphatase was analyzed from cell homogenates, after extraction and solubilization steps. The Vmax and Km values for 4-nitrophenylphosphate at pH = 9.80 were 347.3 +/- 34 IU/ml and 0.7 +/- 0.18 mmol/l, respectively. The pH optimum was 9.80 with 4-nitrophenylphosphate. L-Homoarginine and EDTA, but not L-phenylalanine, inhibited the enzyme. Magnesium above a concentration of 0.5 mmol/l has shown a protective effect against inhibition by 115, 156 and 250 mmol/l urea (final concentration). Sheep neutrophil alkaline phosphatase was found to be very heat-labile. Polyacrylamide gel electrophoresis indicated a single band of activity with a relative mobility similar to that of the slow component of bone and liver isozymes. It is suggested from the above results that sheep neutrophil alkaline phosphatase shares several biochemical properties similar to those of hepatic bone tissue isozyme.
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PMID:Characterization of alkaline phosphatase in polymorphonuclear neutrophils from normal sheep. 323 20

Radiation-inactivation studies were performed on brush-border-membrane vesicles purified from rat kidney cortex. No alteration of the structural integrity of the vesicles was apparent in electron micrographs of irradiated and unirradiated vesicles. The size distributions of the vesicles were also similar for both populations. The molecular sizes of two-brush-border-membrane enzymes, alkaline phosphatase and 5'-nucleotidase, estimated by the radiation-inactivation technique, were 104800 +/- 3500 and 89,400 +/- 1800 Da respectively. Polyacrylamide-gel-electrophoresis patterns of membrane proteins remained unaltered by the radiation treatment, except in the region of higher-molecular-mass proteins, where destruction of the proteins was visible. The molecular size of two of these proteins was estimated from their mobilities in polyacrylamide gels and was similar to the target size, estimated from densitometric scanning of the gel. Intravesicular volume, estimated by the uptake of D-glucose at equilibrium, was unaffected by irradiation. Uptake of Na+, D-glucose and phosphate were measured in initial-rate conditions to avoid artifacts arising from a decrease in the driving force caused by a modification of membrane permeability. Na+-independent D-glucose and phosphate uptakes were totally unaffected in the dose range used (0-9 Mrad). The Na+-dependent uptake of D-glucose was studied in irradiated vesicles, and the molecular size of the transporter was found to be 288,000 Da. The size of the Na+-dependent phosphate carrier was also estimated, and a value of 234,000 Da was obtained.
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PMID:Radiation-inactivation studies on brush-border-membrane vesicles. General considerations, and application to the glucose and phosphate carriers. 342 23

Clinical laboratory tests are increasingly being used to evaluate individuals for osteoporosis and other metabolic bone diseases. Serum bone alkaline phosphatase (AP) [EC 3.1.3.1, orthophosphoric-monoester phosphohydrolase (alkaline optimum)] and osteocalcin are used to assess osteoblastic activity. Although methods for assessing relative amounts of AP isoenzymes continuously appear in the literature, no single method is satisfactory for quantification. Polyacrylamide gel electrophoresis with densitometric scanning combined with two-point heat inactivation was used to obtain quantitative values for AP isoenzymes. Serum bone AP concentrations correlated positively and significantly with serum osteocalcin concentrations obtained by radioimmunoassay for women. Men had significantly higher total alkaline phosphatase and bone AP than women, whereas liver AP concentrations did not differ between the two groups. Bone AP correlated negatively and significantly with age in men, but not women. Osteocalcin concentrations tended to be higher in men, but not significantly.
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PMID:Alkaline phosphatase isoenzymes and osteocalcin in serum of normal subjects. 349 7


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