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PubMed1976

Isolation and properties of a small manganese-ion-stimulated bacterial alkaline phosphatase.

1. An alkaline phosphatase was partially purified from extracts of Halobacterium cutirubrum. 2. The enzyme has a mol.wt. of 15 500 and is therefore less than one-quarter of the size of other known bacterial alkaline phosphatases. 3. It is stimulated up to ten-fold by Mn2+, but not by Ca2+ or Mg2+. 4. The activities with and without Mn2+ cannot be separated by gel filtration and have similar restricted substrate specificities. 5. The only substrates for the enzyme that have so far been found are p-nitrophenyl phosphate, 5'-dATP, 5'-dTMP and 5'-dTTP.

Adenosine Triphosphate↗
PubMed1987

Hydrolysis of phosphatidate by human placental alkaline phosphatase.

Highly purified alkaline phosphatase of human placenta catalyzed the hydrolysis of phosphatidate with quantitative formation of almost stoichiometric amounts of diglyceride and inorganic phosphate. In the presence of sodium deoxycholate, the activity was maximal at pH 8.8. The activity was strongly inhibited by L-phenylalanine but scarcely affected by NaF. These results show that alkaline phosphatase hydrolyzes phosphatidate under different conditions from those for activity of phosphatidate phosphohydrolase.

Alkaline Phosphatase↗
PubMed1985

The relationship of alkaline phosphatase, CaATPase, and phytase.

Alkaline phosphatase, highly purified from bovine intestinal mucosa, has significant hydrolytic activity against phytate and CaATP. Phytase and CaATPase activities require quite different assay conditions than those which are optimal for conventional alkaline phosphatase substrates such as 4-nitrophenyl phosphate. We have used affinity chromatography and antibody recognition to demonstrate that the phytase and CaATPase activities are not due to contaminating enzymes, but are intrinsic activities of intestinal alkaline phosphatase. All of the phytase and CaATPase activities present in crude extracts of bovine intestinal mucosa can be accounted for by alkaline phosphatase. Apparently neither phytase nor CaATPase exist in this tissue as independent enzymes. Specific substrates which require assay conditions quite different from the conventional 4-nitrophenyl phosphate substrate may account for the physiological function of "alkaline phosphatase."

6-Phytase↗
PubMed1981

Periodate-oxidized AMP as a substrate, an inhibitor and an affinity label of human placental alkaline phosphatase.

Human placental alkaline phosphatase (EC 3.1.3.1) was inactivated by periodate-oxidized AMP. The inactivation showed saturation kinetics and could be partially prevented by the substrate AMP or the product inhibitor inorganic phosphate. Oxidized AMP was itself a substrate for this enzyme, with an apparent Km of 0.67 mM. The hydrolytic products of oxidized AMP were identified as oxidized adenosine hemiacetals. Oxidized AMP was also found to be a non-competitive inhibitor with respect to p-nitrophenyl phosphate, with identical Kis and Kii values of 0.15 mM. Our results indicate that oxidized AMP could combine with the enzyme to form a binary complex, followed by reaction with the proximal lysyl amino group to yield a Schiff base. The latter was reduced with NaBH4 and identified by t.l.c. The incorporation of only 1.5 molecules of oxidized [14C]AMP per enzyme subunit resulted in a complete inactivation of the enzyme. The modified enzyme showed higher apparent Km for the substrates and higher Ki for inorganic phosphate, but lower [32P]phosphate incorporation, than the native enzyme. These results support the conclusion that a lysine residue is involved in the phosphate-binding site of human placental alkaline phosphatase.

Adenosine Monophosphate↗
PubMed1987

Purification and partial amino acid sequencing of bovine kidney alkaline phosphatase.

Bovine kidney alkaline phosphatase (ALPase) was purified by the sequential application of monoclonal anti-bovine cartilage ALPase affinity, DEAE-cellulose, and Sepharose CL-6B chromatography. Sodium dodecyl sulfate-polyacrylamide-gel electrophoresis showed the presence of a single band corresponding to a molecular weight of 80,000. The N-terminal amino acid sequence of bovine kidney alkaline phosphatase was determined as follows: Leu-Val-Pro-Glu-Lys-Asp-Pro-?-Tyr-Trp-Arg-Asp-Gln-Ala-Gln.

Alkaline Phosphatase↗
PubMed1987

Association of high-molecular-mass and electrophoretically atypical alkaline phosphatases.

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.

Adolescent↗
PubMedDate not supplied

Osteosarcoma cells in tissue culture: II. Characterization and localization of alkaline phosphatase activity.

Although elevated alkaline phosphatase levels in osteosarcoma have been shown to be related to prognosis, the functional significance is unclear. Human osteosarcoma cells in tissue culture retain detectable amounts of alkaline phosphatase activity. In this study the specific activity of that enzyme was compared in 13 osteosarcoma tissue culture lines and 13 normal skin fibroblast lines derived from the same patients. Osteosarcoma cells had significantly higher baseline alkaline phosphatase levels and could be stimulated with hydrocortisone to produce more enzymatic activity than the fibroblast lines. Activity was localized ultracytochemically to the cell membrane and to many small intracellular vesicles in stimulated osteosarcoma cells. These observations aid in the differentiation of osteosarcoma and fibroblast lines in tissue culture and suggest an association between elevated alkaline phosphatase levels and metabolic abnormalities in patients with osteosarcoma.

Acid Phosphatase↗
PubMed1984

Induction of placental alkaline phosphatase biosynthesis by sodium butyrate.

Placental alkaline phosphatase activity was induced in choriocarcinoma cells by sodium butyrate. Butyrate stimulated de novo synthesis of the enzyme and the increase in phosphatase activity could be completely accounted for by the increase in phosphatase protein: the increases in placental alkaline phosphatase immunoactivity and placental alkaline phosphatase biosynthesis as measured by incorporation of the radioactive precursors, L-[35S]methionine, [3H]mannose, and [3H] glucosamine were similar to the increase in phosphatase activity. Sodium butyrate increased the rates of placental alkaline phosphatase biosynthesis but had no effect on the rate of placental alkaline phosphatase degradation or processing. Both control and butyrate-induced cells contained polypeptides of 61,500 and 64,500 apparent molecular weights that were identified as the precursor and fully processed forms of the placental alkaline phosphatase monomer, respectively. Further, processing of the 61,500-dalton polypeptide to the 64,500-dalton polypeptide involved the incorporation of additional glucosamine and N-acetylneuraminic acid moieties. Gel electrophoresis of anti-placental alkaline phosphatase-precipitable polypeptides from an in vitro protein-synthesizing system directed by RNA isolated from control or butyrate-induced cells demonstrated that sodium butyrate induced the synthesis of placental alkaline phosphatase mRNA. Our data indicate that sodium butyrate induces the specific transcription of the placental alkaline phosphatase gene.

Alkaline Phosphatase↗
PubMed1996

The measurement of acid and alkaline phosphatase in gingival crevicular fluid during orthodontic tooth movement.

This study examines acid and alkaline phosphatase activities in gingival crevicular fluid (GCF) to learn whether bone turnover dynamics can be monitored in human subjects during orthodontic tooth movement. Three female subjects were observed longitudinally to assess tooth movement, plaque, and inflammation. For each subject, one randomly selected premolar served as the control and was not treated, and another was moved buccally with 100 gm of force. The GCF was collected weekly and assayed for phosphatases. Alkaline phosphatase peaked between the first and third weeks, followed by an increase in acid phosphatase between the third and sixth weeks. After the first week, tooth movement averaged 0.9 mm. Additional 0.9 mm of movement occurred during the next 3 weeks, followed by 1.4 mm during weeks 4 to 6. Thirty additional patients, randomly divided into headgear/biteplate, bionator, and control groups, were also sampled cross-sectionally at the maxillary first molars. The GCF phosphatase activities were assessed as functions of location on the tooth, treatment modality, duration of treatment, gingival inflammation, and plaque accumulation. The plaque index did not show a relationship to either acid or alkaline phosphatase activity on the mesial or distal in the treated groups. However, alkaline phosphatase increased with inflammation on the distal in treated groups and acid phosphatase was consistently higher on the mesial than on the distal in the treatment groups. Alternating peaks of acid and alkaline phosphatase were found in the GCF of treated teeth as functions of treatment duration. The sequence of these changes is similar to that reported for alveolar bone turnover in a rodent orthodontic tooth movement model. We conclude that phosphatase activities in GCF may be a useful means for monitoring tissue responses to orthodontic treatment.

Acid Phosphatase↗
PubMedDate not supplied

[Retrospective marker analyses performed with blood and bone marrow smears using an immunoenzyme procedure (alkaline phosphatase-anti-alkaline phosphatase technic)].

In the present study the possibility of immunophenotyping of routinely prepared (air dried) peripheral blood and bone marrow smears is described after storage. The immunoenzymatical alkaline-phosphatase-anti-alkaline-phosphatase (APAAP)-method was carried out in differently stored blood smears (+4 degrees C and -80 degrees C). Last results were compared with originals made from freshly prepared mononuclear cells at time of diagnosis. The results showed no remarkable decrease of antigenicity, neither under the procedure refrigeration and thawing of the frozen smears (-80 degrees C), nor under storage conditions of more than 22 months. In our opinion this highly sensitive method enables us to get additional results from unexplained haematological disorders using retrospective analysis.

Antibodies, Monoclonal↗
PubMed1975

Regulation of Escherichia coli K10 aminoendopeptidase synthesis. Effects of mutations involved in the regulation of alkaline phosphatase.

The synthesis of alkaline phosphatase in Escherichia coli is controlled by the action of at least four genes denoted phoS, phoT, phoR and phoB. The effect of mutations in the first three of these genes on the synthesis of periplasmic aminoendopeptidase of E. coli K 10 have been investigated. phoR gene product does not seem to be involved either in the constitutive or in the derepressed synthesis of this enzyme. Mutations in phoS or phoT influence the intracellular level of Pi in much the same way as depletion of Pi from the growth medium, and only as a consequence influence the synthesis of aminoendopeptidase and alkaline phosphatase. Point, amber or deletion mutations in the alkaline phosphatase structural gene do not affect aminoendopeptidase synthesis. Thus, alkaline phosphatase and 'derepressed' aminoendopeptidase synthesis are co-regulated by the endogenous level of inorganic phosphate. The way by which this regulation operates is discussed.

Alkaline Phosphatase↗