PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “ALKALINE PHOSPHATASE”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

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

At least 37 records · Page 2Linked to original sources
PubMed1993

Effects of the (1-34) fragment of synthetic parathyroid hormone-related protein on tartrate-resistant acid phosphatase and alkaline phosphatase and alkaline phosphatase activities, and on osteocalcin synthesis, in cultured fetal rat calvaria.

In the last years, a parathyroid hormone (PTH)-related peptide (PTHrP) has been isolated from tumors associated with humoral hypercalcemia with malignancy (HHM). In the present work, we studied the effect of bovine PTH (bPTH)(1-34) and PTHrP(1-34) on tartrate-resistant acid phosphatase (TRAP), a marker of bone resorption, and alkaline phosphatase (AP) activities, and basal and vitamin D-stimulated osteocalcin (BGP) synthesis (markers of bone formation) in fetal rat calvaria cultures. After a 48-hour incubation period, both bPTH(1-34) and PTHrP(1-34) caused an increase in TRAP activity liberated in the medium with respect to control cultured calvaria. On the other hand, while after 2 or 4 h of incubation both bPTH(1-34) and PTHrP(1-34) caused a decrease in the AP activity liberated in the medium, after 48 h of incubation both peptides caused a significant increase in the AP liberated in the medium with respect to control cultures. With respect to BGP synthesis, both bPTH(1-34) and PTHrP(1-34) antagonized the 1,25-dihydroxyvitamin D3 stimulatory effect in calvaria cultures. We conclude that PTHrP(1-34) causes similar effects on bone, in organ cultures, to those caused by bPTH(1-34), namely an increase in both bone resorption and formation and a decrease in the vitamin D-stimulated BGP synthesis.

Acid Phosphatase↗
PubMed1977

Alkaline phosphatase and alkaline phosphatase isoenzymes in the cat.

Feline alkaline phosphatase and alkaline phosphatase isoenzymes have been studied in tissue and serum. Alkaline phosphatase from various organs was quantitated and then subjected to cellulose acetate electrophoresis. The effects of bile duct ligation, prednisolone treatment and phenobarbital treatment on serum alkaline phosphatase was measured. The diagnostic importance of feline serum alkaline phosphatase levels is discussed in light of the results of this and other studies.

Journal Article↗
PubMed1998

Sensitivity and specificity of indirect immunofluorescence and Grocott-technique in comparison with immunocytology (alkaline phosphatase anti alkaline phosphatase = APAAP) for the diagnosis of Pneumocystis carinii in broncho-alveolar lavage (BAL).

The purpose of the study was to compare the sensitivity and specificity of the indirect method of immunofluorescence with the immunocytological technique of alkaline phosphatase anti alkaline phosphatase complex (APAAP) for the detection of Pneumocystis carinii by bronchoalveolar lavage (BAL) in HIV-1 positive patients. - 83 HIV-1 positive patients with clinical presentations suggestive of Pneumocystis carinii pneumonia (PcP) were included in the study. 28 samples were found Pc-positive by immunofluorescence (IFT), 26 by Grocott and 29 by APAAP. In comparison to the lab results 33 patients were diagnosed as PcP according to the clinical course (i.e. therapeutic outcome, drugs used, and therapy changes). Compared to the clinical diagnoses, the following lab tests proved to be false positive and false negative: false positive: IF = 1, Grocott = 0, APAAP = 4 (3F6). false negative: IF = 5, Grocott = 7, APAAP = 4 (3F6). - Grocott stain shows insufficient correlation to the clinical diagnoses (p = 0.0156, McNemar-Test, two-tailed). - The two different detection methods (IFT and APAAP) showed no significant statistical difference with regard to their sensitivity (p = 0.3438, McNemar-Test, two tailed) and specificity. Considering cost and time the immunofluorescence technique seems to be the most suitable for the diagnosis of PcP in HIV-1 positive patients.

AIDS-Related Opportunistic Infections↗
PubMed1990

High-molecular-weight alkaline phosphatase and alkaline phosphatase lipoprotein X complex in cholestasis and hepatic malignancy.

Alkaline phosphatase (ALP) fast liver isoenzyme is now known as high-molecular-weight ALP. This ALP isoenzyme represents fragments of hepatic cell plasma membranes with various membrane-bound enzymes localized on the surface. High-molecular-weight ALP isoenzyme is present in patients' serum samples in conditions associated with intrahepatic and extrahepatic cholestasis and primary or metastatic hepatic malignancy. High-molecular-weight ALP isoenzyme may coexist with ALP of the normal liver and with ALP lipoprotein X. Alkaline phosphatase ultrafast liver isoenzyme is now known as ALP lipoprotein X complex.

Adult↗
PubMed1967

Alkaline inorganic pyrophosphatase activity of mammalian-cell alkaline phosphatase.

Alkaline phosphatase prepared from mammalian cell cultures was found to have alkaline inorganic pyrophosphatase activity. Both of these activities appear to be associated with a single protein, as demonstrated by: (1) concomitant purification of alkaline phosphatase and alkaline inorganic pyrophosphatase; (2) proportional precipitation of alkaline phosphatase and inorganic pyrophosphatase activities by titrating constant amounts of an enzyme preparation with increasing concentration of antibody; (3) immune electrophoresis, which showed that precipitin bands that have alkaline phosphatase activity also have pyrophosphatase activity; (4) inhibition of pyrophosphatase activity by cysteine, an inhibitor of alkaline phosphatase activity; (5) similar subcellular localization of the two enzyme activities as demonstrated by histochemical methods; (6) hormonal and substrate induction of alkaline phosphatase activity in mammalian cell cultures, which produced a nearly parallel rise in inorganic pyrophosphatase activity.

Alkaline Phosphatase↗
PubMed1987

Phosphatidylinositol anchor of HeLa cell alkaline phosphatase.

Alkaline phosphatase from cancer cells, HeLa TCRC-1, was biosynthetically labeled with either 3H-fatty acids or [3H]ethanolamine as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography of immunoprecipitated material. Phosphatidylinositol-specific phospholipase C (PI-PLC) released a substantial proportion of the 3H-fatty acid label from immunoaffinity-purified alkaline phosphatase but had no effect on the radioactivity of [3H]ethanolamine-labeled material. PI-PLC also liberated catalytically active alkaline phosphatase from viable cells, and this could be selectively blocked by monoclonal antibodies to alkaline phosphatase. However, the alkaline phosphatase released from 3H-fatty acid labeled cells by PI-PLC was not radioactive. By contrast, treatment with bromelain removed both the 3H-fatty acid and the [3H]ethanolamine label from the purified alkaline phosphatase. Subtilisin was also able to remove the [3H]ethanolamine-labeled from purified alkaline phosphatase. The 3H radioactivity in alkaline phosphatase purified from [3H]ethanolamine-labeled cells comigrated with authentic [3H]ethanolamine by anion-exchange chromatography after acid hydrolysis. The data suggest that the 3H-fatty acid and [3H]ethanolamine are covalently attached to the carboxyl-terminal segment since bromelain and subtilisin both release alkaline phosphatase from the membrane by cleavage at that end of the polypeptide chain. The data are consistent with findings for other proteins recently shown to be anchored in the membrane through a glycosylphosphatidylinositol structure and indicate that a similar structure contributes to the membrane anchoring of alkaline phosphatase.

Alkaline Phosphatase↗
PubMed2002

The 1.9 A crystal structure of heat-labile shrimp alkaline phosphatase.

Alkaline phosphatases are non-specific phosphomonoesterases that are distributed widely in species ranging from bacteria to man. This study has concentrated on the tissue-nonspecific alkaline phosphatase from arctic shrimps (shrimp alkaline phosphatase, SAP). Originating from a cold-active species, SAP is thermolabile and is used widely in vitro, e.g. to dephosphorylate DNA or dNTPs, since it can be inactivated by a short rise in temperature. Since alkaline phosphatases are zinc-containing enzymes, a multiwavelength anomalous dispersion (MAD) experiment was performed on the zinc K edge, which led to the determination of the structure to a resolution of 1.9 A. Anomalous data clearly showed the presence of a zinc triad in the active site, whereas alkaline phosphatases usually contain two zinc and one magnesium ion per monomer. SAP shares the core, an extended beta-sheet flanked by alpha-helices, and a metal triad with the currently known alkaline phosphatase structures (Escherichia coli structures and a human placental structure). Although SAP lacks some features specific for the mammalian enzyme, their backbones are very similar and may therefore be typical for other higher organisms. Furthermore, SAP possesses a striking feature that the other structures lack: surface potential representations show that the enzyme's net charge of -80 is distributed such that the surface is predominantly negatively charged, except for the positively charged active site. The negatively charged substrate must therefore be directed strongly towards the active site. It is generally accepted that optimization of the electrostatics is one of the characteristics related to cold-adaptation. SAP demonstrates this principle very clearly.

Alkaline Phosphatase↗
PubMedDate not supplied

Combination of alkaline phosphatase anti-alkaline phosphatase (APAAP)- and avidin-biotin-alkaline phosphatase complex (ABAP)-techniques for amplification of immunocytochemical staining of human testicular tissue.

An amplification procedure was developed for the visualization of antigens in human testis using monoclonal antibodies against desmin and vimentin. The technique combines the high sensitive and specific APAAP- and ABAP-methods. Depending on the quality of the antibodies used and the processing of the material prior to the immunocytochemical staining the amplification technique may be applied either as a single APAAP and ABAP- or as a double APAAP and ABAP-combination. Especially after the double amplification reaction a distinct increase of the staining intensity of the vimentin- (in Sertoli cells, myofibroblasts of the lamina propria, and fibroblasts of the interstitium) and desmin- (in myofibroblasts of the lamina propria and smooth muscle cells of the blood vessels) like immunoreactivity was observed. If different diazonium salts were used for the visualization of the alkaline phosphatase activity (e.g. Fast Red TR Salt, Fast Blue BB Salt) desmin- and vimentin-like immunoreactivity can be demonstrated in the same tissue section in a double sequential staining approach. For double staining, the alkaline phosphatase technique may be combined successfully with a technique or a combination that uses peroxidase as a marker.

Alkaline Phosphatase↗
PubMed1965

HEAT STABILITY OF HUMAN PLACENTAL ALKALINE PHOSPHATASE.

Alkaline phosphatase prepared from human placentae shows greater resistance to heat inactivation than any other known alkaline phosphatase of human origin. In the presence of magnesium this enzyme may be heated at 70 degrees C. for 30 minutes without loss of activity whereas other human alkaline phosphatases lose most of their activity on being heated at 56 degrees C. for this period of time. This heat stability is seen in freshly prepared enzyme, in alcohol-fractionated and freeze-dried material, and in the sera of individuals into whom placental alkaline phosphatase has been infused. The clinical implications of our observations are briefly indicated.

Alkaline Phosphatase↗
PubMed1983

Analytical subcellular fractionation of rat pituitary homogenates with special reference to the subcellular localization and properties of alkaline phosphatases.

Alkaline phosphatase activities of the virgin rat anterior pituitary were studied with a highly sensitive fluorometric assay. Tissue whole homogenates were fractionated on sucrose density gradients in a Beaufay automatic zonal rotor and the gradient fractions assayed for alkaline phosphatase, prolactin and various organelle marker enzymes. Alkaline phosphatase was distributed between two peaks on the gradient. The low-density (1.10-1.15 g . cm-3) alkaline phosphatase component co-sedimented with the plasma membrane marker, 5'-nucleotidase, had an apparent Km for 4-methylumbelliferyl phosphate of approx. 59 microM, and was inhibited by levamisole. The high-density (1.20-1.25 g . cm-3) peak was resistant to levamisole-inhibition, had an apparent Km of approx. 30 microM and its distribution was distinct from plasma membrane, Golgi, lysosome, endoplasmic reticulum, mitochondria and prolactin granule markers on the isopycnic gradients.

Alkaline Phosphatase↗
PubMed1978

Effects of experimental diabetes and food intake on rat intestine and serum alkaline phosphatase.

Alkaline phosphatase activity of rat serum was reduced 50% by fasting the animal for 24 hours. Diabetes, induced by alloxan or streptozotocin, increased serum alkaline phosphatase 3- to 5-fold in fed rats and the elevated activity was reduced by insulin administration. In the absence of insulin, fasting alone was able to reduce the serum alkaline phosphatase of diabetic rats to control values. The elevated serum isozyme was found to be of intestinal origin by the use of appropriate inhibitors and electrophoretic mobility following neuraminidase treatment. It is concluded that food intake, particularly the hyperphagia of diabetes, plays a major role in regulating the concentration of intestine and serum alkaline phosphatase in the rat.

Alkaline Phosphatase↗
PubMed1993

The effect of carbohydrate additives in the freeze-drying of alkaline phosphatase.

Alkaline phosphatase was used as a model in studies to assess the effects of lyophilization on biological activity and molecular integrity in the presence or absence of added carbohydrate. The stability of the activity of alkaline phosphatase, lyophilized in Tris buffer alone or in the presence of the carbohydrates mannitol, lactose or trehalose was examined. Enzyme activity in formulations with Tris buffer alone or with mannitol was considerably reduced by freeze-drying and further storage at elevated temperatures; freeze-drying with mannitol failed to maintain activity at a temperature of 37 degrees C over 21 days, whilst the loss of activity was more gradual when freeze-dried in buffer alone and stored at higher temperatures. Lactose and trehalose maintained the alkaline phosphatase activity after freeze-drying and, furthermore, preparations containing trehalose retained activity even when the material was subjected to temperatures of up to 45 degrees C for up to 84 days. At 56 degrees C the alkaline phosphatase activity did not show a significant drop until 14 days with the lactose formulation or until 21 days with trehalose. After 84 days at 56 degrees C, 30% of the activity still remained in the formulation containing trehalose. In addition to the changes in the enzyme activity, FPLC chromatographic traces and SDS-PAGE gels demonstrated compositional differences between each formulation after storage.

Alkaline Phosphatase↗