Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “ALKALINE PHOSPHATASE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,189 records · Page 66Linked to original sources
PubMed1981

Extracellular alkaline phosphatase from alveolar secretions of patients with pulmonary alveolar proteinosis.

Alkaline phosphatases in alveolar secretions from the lungs of patients with pulmonary alveolar proteinosis have been studied. A soluble form of alkaline phosphatase was isolated from the secretions and characterized. The extracellular enzyme had a pH optimum at 9.95; was stimulated by Mg2+, Ni2+, and Mn2+; was inhibited by Zn2+, Be2+, Cu2+, and low concentrations (8 mM) of L-homoarginine and imidazole; and was heat-stable at 55 degrees C. The soluble phosphatase existed primarily as a high molecular weight complex (excluded from Sepharose 4B) and could be dispersed into low molecular weight forms (205 000--285 000) by treatment with n-butanol. Following butanol treatment, the thermostability of the enzyme was markedly decreased but the kinetic properties such as the Km values, activation energies, and responses to various inhibitors were unchanged. The alkaline phosphatase may originate from unusual type 2 cells present in the alveoli of patients with pulmonary alveolar proteinosis.

Alkaline Phosphatase↗
PubMed1975

Acid and alkaline phosphatases in the kidney of a few fishes.

The localization of acid and alkaline phosphatases in the kidney of Cirrhinus reba, Ompak bimaculatus and Labeo gonius has been studied. In all these fishes, the enzymes are found in the proximal tubule. The activity of alkaline phosphatase is more stronger than acid phosphatase. The renal capsule, distal tubule, collecting tubule and interstitial hematopoietec tissue are all phosphatase negative. The activity is more stronger in the first proximal tubule than in the second tubule. It is probable that acid phosphatase is associated with the intracellular digestion of the macromolecules absorbed and alkaline phosphatase with the absorption of glucose from the tubular lumen.

Acid Phosphatase↗
PubMed1988

Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene.

A full-length placental alkaline phosphatase (PLAP) cDNA was used to identify and clone the PLAP-like Nagao isozyme gene from human genomic libraries. The entire nucleotide sequence of the gene reveals the existence of 11 exons interrupted by 10 small introns (76-427 base pairs). Putative regulatory sequences have been identified in the promoter regions as well as dispersed in the introns. The deduced amino acid sequence of the Nagao isozyme indicates that the mature molecule is composed of 513 amino acids, of which 12 residues are different from the sequence of PLAP (98% homology). A sequence derived from exon III of the Nagao isozyme gene was used to synthesize a peptide (NH2-Lys-Leu-Gly-Pro-Glu-Thr-Phe-Leu-Ala-COOH) that contains two mutations with respect to the corresponding PLAP sequence. This peptide elicited rabbit polyclonal antibodies that reacted specifically with the seminoma Nagao isozyme but not with PLAP in electrophoretic transfer blots. These results indicate that the tumor, and possibly the normal testis, Nagao isozyme is encoded by a gene referred to as germ-cell alkaline phosphatase gene that differs from the PLAP gene expressed by syncitiotrophoblastic cells.

Alkaline Phosphatase↗
PubMed1977

The source and clinical significance of serum alkaline phosphatases in neoplastic blood diseases.

Total serum alkaline phosphatase activity and its isoenzymes were studied in 126 patients sent to hospital with a neoplastic blood disease. They comprised 63 patients with a lymphoreticular neoplastic disease, 17 with immature stem-cell leukaemia, 11 with a plasmocytoma, 16 with lymphocytic leukaemia, 4 with polycythaemia and 9 with the myelofibrosis syndrome. Evaluation of the serum alkaline phosphatase isoenzymes significantly enhances the efficiency of the diagnosis and the organ specificity of the enzymes in these conditions. It is particularly important in the above states for studying liver and bone involvement, both from the aspect of the organic localization of the disease and from the aspect of evaluation of the success of therapy.

Alkaline Phosphatase↗
PubMed2005

A highly active alkaline phosphatase from the marine bacterium cobetia.

An alkaline phosphatase with unusually high specific activity has been found to be produced by the marine bacterium Cobetia marina (strain KMM MC-296) isolated from coelomic liquid of the mussel Crenomytilus grayanus. The properties of enzyme, such as a very high specific activity (15000 DE U/1 mg of protein), no activation with divalent cations, resistance to high concentrations of inorganic phosphorus, as well as substrate specificity toward 5' nucleotides suggest that the enzyme falls in an intermediate position between unspecific alkaline phosphatases (EC 3.1.3.1) and 5' nucleotidases (EC 3.1.3.5).

5'-Nucleotidase↗
PubMed1971

Molecular aspects of the regulation of rat kidney alkaline phosphatase.

The mechanisms by which phosphate regulates the activity of alkaline phosphatase (orthophosphoric monoester phosphohydrolase, EC 3.1.3.1) in rat kidney were investigated. Measurements of incorporation of [(14)C]leucine into kidney alkaline phosphatase in rats fed on complete or phosphate-free diet provide evidence of a twofold increase in the rate of synthesis of the enzyme in diet-treated animals. Cycloheximide experiments indicated that control and diet-adapted enzyme decreases in activity according to first-order kinetics with a calculated half-life of 10.3 and 6.5h after complete and phosphate-free diet administration respectively. Basal and diet-adapted enzymes exhibit similar K(m) values for several phosphomonoesters and an identical degree of inhibition is produced by cysteine. In addition, the enzyme from both sources is the same with regard to heat inactivation at 45, 56 or 64 degrees C, to the profile of elution from Sephadex and to electrophoretic properties on polyacrylamide gel. A failure of rat kidney alkaline phosphatase to respond to cortisol (hydrocortisone) was also observed.

Adrenal Glands↗
PubMed1979

High molecular weight alkaline phosphatase: a clinical study.

High molecular weight alkaline phosphatase activities have been measured in the sera of 72 patients with a variety of forms of liver disease, 14 patients with bone disease and 8 healthy volunteers. These measurements have been compared with measurements of other indices of hepatic function in order to establish the place of this enzyme in the diagnosis of liver disease. High molecular weight alkaline phosphatase proved to be a sensitive and specific tests for detecting liver disease, particularly obstructive liver disease. It was better than all the other liver function tests in distinguishing liver metastases from other hepatobiliary diseases. It may therefore prove especially useful in the early detection of liver metastases.

Adult↗
PubMed1979

Enzymatic characterization of the chondrocytic alkaline phosphatase isolated from bovine fetal epiphyseal cartilage.

Purified chondrocytic alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) from bovine fetal epiphyseal cartilage hydrolyzes a variety of phosphate esters as well as ATP and inorganic pyrophosphate. Optimal activities for p-nitrophenyl phosphate, ATP and inorganic pyrophosphate are found at pH 10.5, 10.0 and 8.5, respectively. The latter two substrates exhibit substrate inhibition at high concentrations. p-Nitrophenyl phosphate demonstrates decreasing pH optima with decreasng substrate concentration. Heat inactivation studies indicate that both phosphorolytic and pyrophosphorolytic cleavage occur at the same site on the enzyme. Mg2+ (0.1-10.0 mM) and Mn2+ (0.01-0.1 mM) show a small stimulation of p-nitrophenyl phosphate-splitting activity at pH 10.5. Levamisole, Pi, CN-, Zn2+ and L-phenylalanine are all reversible inhibitors of the phosphomonoesterase activity. Pi is a competitive inhibitor with a Ki of 10.0 mM. Levamisole and Zn2+ are potent non-competitive inhibitors with inhibition constants of 0.05 and 0.04 mM, respectively. The chondrocytic alkaline phosphatase is inhibited irreversibly by Be2+, EDTA, EGTA, ethane-1-hydroxydiphosphonate, dichloromethane diphosphonate, L-cysteine, phenyl-methylsulfonyl fluoride, N-ethylmaleimide and iodoacetamide. NaCL, KCL and Na2SO4 at 0.5-1.0 M inhibit the enzyme. At pH 8.5, the cleavage of inorganic pyrophosphate (pyrophosphate phosphohydrolase, EC 3.6.1.1) by the chondrocytic enzyme is slightly enhanced by low levels of Mg2+ and depressed by concentrations higher than 1mM. Ca2+ show only inhibition. Similar effects of Mg2+ and Ca2+ on the associated ATPase (ATP phosphohydrolase, EC 3.1.6.3) activity were observed. Arrhenius studies using p-nitrophenyl phosphate and AMP as substrates have accounted for the ten-fold difference in V in terms of small differences in both the enthalpies and entropies of activation which are 700 cal/mol and 2.3 cal/degree per mol, respectively.

Adenosine Triphosphatases↗
PubMedDate not supplied

Histoenzymological mapping of alkaline phosphatase and 5-nucleotidase in the medulla oblongata of a microchiropteran bat (Taphozous melanopogon Temminck).

The contribution deals with the distribution of alkaline phosphatase and 5-nucleotidase in the medulla oblongata of Taphozous melanopogon (a Microchiroptera), for the first time. The main highlights of the study are: (1) Cranial nerve nuclei demonstrate intense activity of alkaline phosphatase, whereas except nucleus tractus spinalis n. trigemini, rest of the nuclei show much variations of 5-nucleotidase distribution. (2) The vestibular nuclei are very intensely positive for 5-nucleotidase but exhibit variable activity of alkaline phosphatase. (3) Three subdivisions of nucleus olivaris inferior, i.e. nucleus olivaris accessorius medialis, nucleus olivaris accessorius dorsalis and nucleus olivaris inferior, which were not reported in the earlier neuroanatomical studies, have been identified. These nuclei show very intense alkaline phosphatase and relatively less intense 5-nucleotidase activities. (4) In general, the activity of alkaline phosphatase is stronger in neurons than in neuropil and that of 5-nucleotidase is stronger in neuropil than in neurons. (5) Blood capillaries are completely negative for alkaline phosphatase and intensely positive for 5-nucleotidase. A comparison is made between the distribution of these enzymes in the medulla oblongata of bat and other mammals so far studied.

Alkaline Phosphatase↗
PubMed1996

Clinical efficacy of bone alkaline phosphatase and prostate specific antigen in the diagnosis of bone metastasis in prostate cancer.

PURPOSE: We investigated the usefulness of bone alkaline phosphatase isoenzyme and prostate specific antigen (PSA) determined by radioimmunoassay to predict bone scan evidence of metastasis in newly diagnosed untreated and treated prostate cancer. MATERIALS AND METHODS: We analyzed bone alkaline enzyme concentrations in 350 men, including 150 controls, 100 with benign prostatic hyperplasia and 100 with prostate cancer (52 with stages T1 to 4, M0 and 48 with stages T1 to 4, M1 to 4). We also analyzed bone alkaline phosphatase enzyme concentrations in 61 stages T1 to 4, M0 prostate cancer cases during followup after radical prostatectomy or hormonal therapy, and 17 had clinical progression (9 with local, 5 with lymph node and 3 with bone metastases). Simultaneously, we analyzed PSA concentrations. RESULTS: Average bone alkaline phosphatase enzyme levels were 12, 11.1 and 10.0 ng./ml. in the control, benign prostatic hyperplasia and stage M0 prostate cancer groups, respectively (p not significant), and 83.2 ng./ml. in patients with stage M1 to 4 disease (p<0.001). Considering that to diagnose bone metastasis the cutoff for bone alkaline phosphatase enzyme and PSA is 30 ng./ml. and 100 ng./ml., respectively, clinical effectiveness was 93.7% and 81.8%, respectively. Finally, measurement of both substances at the same time increased clinical effectiveness to 97.9%. During followup a bone alkaline phosphatase enzyme level that becomes greater than 30 ng./ml. (0% in the local and lymphatic progression groups, and 100% in the bone metastasis group) indicates the need to perform a bone scan. CONCLUSIONS: We recommend the clinical use of bone alkaline phosphatase enzyme determined by radioimmunoassay and PSA measurement for the diagnosis of bone metastases and progression of prostate cancer because of the good sensitivity and specificity.

Aged↗
PubMed1951

The role of alkaline phosphatase in osteogenesis.

The role of alkaline phosphatase in osteogenesis has been investigated by histochemical techniques with particular attention to its relationship to phosphate metabolism and matrix elaboration. The upper tibial epiphysis mainly, and other epiphyses as well of growing rabbits, and the costochondral junctions of newborn human beings were studied, as were bone grafts in growing rabbits. The findings in the newborn human beings were identical with those in the rabbits. Phosphatase activity and free phosphate localization do not universally coincide. The enzyme appears to be intimately related to preosseous cellular metabolism and to the elaboration of a bone matrix that is chemically calcifiable. It remains possible, however, that phosphatase may be in some way involved in making inorganic salts available to the calcifiable matrix. If this function does exist it is a secondary one, since the elaboration of bone matrix, which is always associated with phosphatase activity, can and does occur in the absence of calcification. Calcification may occur later, in the absence of the enzyme. There is evidence to suggest that cartilage matrix is utilized in the formation of bone matrix. Phosphatase is physiologically active only in the presence of living cells. Where it is demonstrable in the absence of living cells, as in the cartilage remnants of the metaphysis, it appears to be physiologically inactive. Since phosphatase is temporarily inactivated in weakly acid media, and readily reactivated by alkaline solutions it is possible that the enzyme might survive in a physiologically inactive state in weakly acid tissues, and yet remain capable of histochemical demonstration in vitro in an alkaline medium. Phosphatase is not related to the disappearance of chondroitin sulfate.

Alkaline Phosphatase↗
PubMed1977

Intestinal alkaline phosphatase in the diagnosis of liver disease.

Alkaline phosphatase isoenzymes have been studied by acrylamide gel disc electrophoresis in 76 patients with liver disorders comprising 15 with an extrahepatic lesion, 53 with an intrahepatic lesion, and eight patients who had features of both intra- and extrahepatic disease. No intestinal band was found in the 15 cases of extrahepatic liver disease, in marked contrast to the patients with intrahepatic lesions in whom an intestinal band was found in 45% of cases. The intrahepatic group was heterogeneous, a high incidence of intestinal bands being found in patients with cirrhosis of the liver. It is concluded that where a raised serum alkaline phosphatase is found in a patient with jaundice, and a gut band is present on electrophoresis, the lesion is likely to be intrahepatic.

Alkaline Phosphatase↗
PubMed1979

The differential effect of magnesium deficiency on isoenzymes of alkaline phosphatase (EC 3.1.3.1) in rat tissues.

1. Alkaline phosphatase (EC 3.1.3.1) from many rat tissues was separated into two or three bands by electrophoresis on polyacrylamide gel. Ten of the bands had different electrophoretic mobilities, but some were present in more than one tissue. 2. Bands from the corresponding tissues of magnesium-deficient and control rats were qualitatively similar, but there were quantitative differences in the distribution of enzyme activity between them. 3. Mg deficiency had differential effects on the absolute activity of individual bands, but two main types of response were observed. There was an increase in the activity of the first bands from liver and kidney, the second band from femur and both bands from spleen, whereas the first band from femur, the first and second bands from intestinal mucosa and the second bands of serum, liver and kidney all decreased in activity during the deficiency. 4. The change in total alkaline phosphatase activity of a tissue during Mg deficiency depended on the ratio between the enzyme components within it.

Alkaline Phosphatase↗
PubMed1975

Hybrids of chemical derivatives of Escherichia coli alkaline phosphatase.

The activities of hybrid dimers of alkaline phosphatase containing two chemically modified subunits have been investigated. One hybrid species was prepared by dissociation and reconstitution of a mixture of two variants produced by chemical modification of the native enzyme with succinic anhydride and tetranitromethane, respectively. The succinyl-nitrotyrosyl hybrid was separated from the other members of the hybrid set by DEAE-Sephadex chromatography and then converted to a succinyl-aminotyrosyl hybrid by reduction of the modified tyrosine residues with sodium dithionite. A comparison of the activities of these two hybrids with the activities of the succinyl, nitrotyrosyl and aminotyrosyl derivatives has shown that either the subunits of alkaline phosphatase function independently or if the subunits turnover alternately in a reciprocating mechanism, then the intrinsic activity of each subunit must be strongly dependent on its partner subunit.

Alkaline Phosphatase↗
PubMed1976

31P nuclear magnetic resonance study of alkaline phosphatase: the role of inorganic phosphate in limiting the enzyme turnover rate at alkaline pH.

31P nuclear magnetic resonance (NMR) was used to directly observe the binding of inorganic phosphate to alkaline phosphatase. Evidencq for the tight binding of 1.5-2.0 mol of inorganic phosphate per dimer of alkaline phosphatase is presented. Two distinct forms of bound phosphate are observed, one predominating above pH 7 and representing the non-covalent E-P1 complex and the other predominating below pH 5 and representing the covalent E-P1 complex. The 31P NMR line width of the E-P1 complex indicates that the dissociation of noncovalent phosphate is the rate-limiting step in the turnover of the enzyme at high pH.

Alkaline Phosphatase↗
PubMed1972

Escherichia coli alkaline phosphatase. Kinetic studies with the tetrameric enzyme.

1. The stability of the tetrameric form of Escherichia coli alkaline phosphatase was examined by analytical ultracentrifugation. 2. The stopped-flow technique was used to study the hydrolysis of nitrophenyl phosphates by the alkaline phosphatase tetramer at pH7.5 and 8.3. In both cases transient product formation was observed before the steady state was attained. Both transients consisted of the liberation of 1mol of nitrophenol/2mol of enzyme subunits within the dead-time of the apparatus. The steady-state rates were identical with those observed with the dimer under the same conditions. 3. The binding of 2-hydroxy-5-nitrobenzyl phosphonate to the alkaline phosphatase tetramer was studied by the temperature-jump technique. The self-association of two dimers to form the tetramer is linked to a conformation change within the dimer. This accounts for the differences between the transient phases in the reactions of the dimer and the tetramer with substrate. 4. Addition of P(i) to the alkaline phosphatase tetramer caused it to dissociate into dimers. The tetramer is unable to bind this ligand. It is suggested that the tetramer undergoes a compulsory dissociation before the completion of its first turnover with substrate. 5. On the basis of these findings a mechanism is proposed for the involvement of the alkaline phosphatase tetramer in the physiology of E. coli.

Alkaline Phosphatase↗
PubMedDate not supplied

Value of serum alkaline phosphatase in evaluating hyperplasia of parathyroid glands in chronic hemodialysis patients.

To investigate the value of serum alkaline phosphatase in evaluating hyperplasia of parathyroid glands in hemodialysis patients, 28 hemodialysis patients who had parathyroid sonography examinations for secondary hyperparathyroidism were studied retrospectively. There were significant elevations of serum alkaline phosphatase, parathyroid hormone (PTH), serum total calcium, and dialysis duration in patients with sonography-detectable parathyroid (N = 17) as compared with those of sonography-undetectable (N = 11) parathyroid. Hemodialysis patients who have both higher serum alkaline phosphatase (> 94 IU/L) and considerably elevated serum PTH (9 x or higher) are likely to have sonography-detectable parathyroids (positive predictive value of 93%). Patients with mildly or moderately elevated serum PTH but normal serum alkaline phosphatase are less likely to have sonography-detectable parathyroids (negative predictive value is 100%). These findings suggest that the elevation of serum alkaline phosphatase could be a valuable parameter in addition to the high serum PTH level in predicting hyperplasia of parathyroid glands in chronic hemodialysis patients.

Adult↗
PubMed1996

[Isolation and certain properties of mutant alkaline phosphatase of Escherichia coli].

Natural and mutant alkaline phosphatases with amino acid substitutions in the processing site and N-terminal domain of the mature polypeptide chain Val for Ala(-1), Gln for Glu (+4) and simultaneously Gln for Glu (+4) and Ala for Arg (+1) have been isolated from the periplasm and cultural fluid of E. coli. It has been found that these substitutions have little effect on the dependence of the enzyme activity on pH, ionic strength and temperature but influence its isoenzymic spectrum and decrease (almost twofold) the maximal rate of the enzyme-catalyzed reaction. Extracellular enzymes display, in contrast with periplasmic ones, other catalytic properties (Vmax) and binding activity (Km). After translocation through the outer membrane all the enzymes display decreased Vmax and increased Km. These changes are especially well-pronounced in case of the mutant protein PhoA46 which contains an uncleaved signal peptide due to the impossibility of processing resulting from the substitution of Val for Ala(-1). The Vmax for this protein is decreased 20 times, while the Km is increased 4-fold. The protein also shows a higher (in comparison with other proteins) sensitivity towards proteolytic enzymes and is less resistant upon storage. The experimental data suggest that the changes in the N-end of alkaline phosphatase located at a long distance from its active center influence the enzyme function.

Alkaline Phosphatase↗