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)

Procollagen 1 carboxyterminal peptide (P1CP) is thought to be an indicator of new bone formation. The present report demonstrates that effective endocrine therapy induced an initial increase followed by a delayed decrease in serum levels of P1CP and alkaline phosphatase in spite of an immediate decrease in serum PSA and PAP and improvement of clinical symptoms in prostate cancer patients with bone metastases. The transient increase in P1CP and alkaline phosphatase is a healing reaction and is followed by apparent improvement. Short-term effects of endocrine therapy on prostate cancer patients with bone metastases should be comprehensively evaluated based upon the entire spectrum of clinical and laboratory findings including serial changes of serum prostate markers and bone markers as well.
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PMID:A transient increase in serum procollagen 1 carboxyterminal peptide following effective treatment in prostate cancer patients with bone metastases. 925 25

The reference values of common blood chemistry analytes in healthy population, aged newborn to 80 years, of Rawalpindi Islamabad area were determined at AFIP, Rawalpindi. A total of 2115 healthy subjects, 1206 males and 909 females, were included in the study. Plasma glucose was analysed by GOD/POD, serum cholesterol by CHOD/PAP, triglycerides by GPO/PAP, urea by urease/GLDH, creatinine by Jaffe' rate reaction, uric acid by uricase, total bilirubin by Jendrassik and Grof, total protein by biuret, alanine transaminase (ALT) by optimized IFCC and alkaline phosphatase (AP) by optimized DGKC method. The between batch CVs of all the parameters were within acceptable quality goals. The reference values were calculated using 2.5 and 97.5 percentiles as lower and upper limits (95% CI). In healthy adult males the reference values were: fasting plasma glucose, 3.6-6.0 mmol/l; serum cholesterol; 3.2-6.6 mmol/l; triglycerides, 0.6-2.3 mmol/l; urea, 2.8-6.4 mmol/l; creatinine, 65-132 umol/l; uric acid, 164-430 umol/l; total bilirubin, 5-18 umol/l; total protein, 57-83 g/l; ALT, 15-45 U/l and AP, 185-620 U/l. The values in adult females, children and elderly subjects were slightly different than adult males. The reference values of our population show mild to moderate differences from the other Asian, European and American populations. It is recommended that reference values of different biochemical investigations should be established in various areas of Pakistan to make appropriate use of such investigations.
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PMID:Reference values of common blood chemistry analytes in healthy population of Rawalpindi-Islamabad area. 930 Nov 67

The present study was carried out to find the effects of Pb acetate (10-50 mg/kg body wt) after oral administration on: 1. The distribution of elements, such as Fe, Cu, Zn, and Mn; 2. The activity of 6-amino levulenic acid dehydratase (delta-ALAD) and alkaline phosphatase (PAP); and 3. On the level of reduced glutathione (GSH) in murine placenta. Pb toxicity expressed on a dry-wt basis was reflected in terms of deficiency of delta-ALAD and PAP and enhanced content of GSH. Analysis of trace elements following Pb exposure showed low levels of Mn and Cu. Although Fe composition of placenta remained within normal range with increasing load of endogeneous Pb, Zn decline was not consistent after oral feeding of Pb acetate. Deficiency of PAP after Pb exposure did not correlate with the endogeneous levels of Pb or Zn therein, but correlated with endogeneous levels of Mn. Placental deficiencies of Cu and Mn have been related to the disturbed placental functions by Pb accumulation.
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PMID:Trace metals and metalloenzymes in placenta after oral administration of lead acetate. 940 84

A screen-printed carbon electrode (SPCE) has been investigated as the base transducer for a disposable amperometric progesterone biosensor. The biorecognition element was a monoclonal sheep anti-progesterone antibody (mAb). This was immobilized onto the transducer by interaction with a layer of rabbit IgG which had been previously coated onto the SPCE; optimum conditions for these loadings were deduced experimentally. The device was employed in a competitive assay using alkaline phosphatase-labelled progester-one. Three possible substrates for the enzyme were considered, namely, phenyl phosphate, phenolphthalein phosphate and 4-aminophenol phosphate. Cyclic voltammetry and amperometry were carried out on the corresponding aromatic phenols and phenol itself was found to give the best electrochemical characteristics; consequently, phenyl phosphate was employed as the substrate. Chronoamperometry was used to measure the phenol produced by the reaction of bound enzyme-labelled progesterone and substrate. The chronoamperometric response was dependent on unlabelled progesterone over at least three orders of magnitude with a detection limit of about 1 x 10(-9) mol/dm3. This suggests that the device may have applications for the analysis of biological fluids.
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PMID:Studies towards a disposable screen-printed amperometric biosensor for progesterone. 945 99

4-Aminophenyl phosphate (4-APP) and 1-naphthyl phosphate (1-NP) were compared as enzyme substrates for an amperometric milk progesterone biosensor utilising progesterone-conjugated alkaline phosphatase in a competitive immunoassay format. Cyclic voltammetry of the corresponding hydrolysis products, 4-aminophenol and 1-naphthol, at the surface of screen-printed carbon base transducers, uncoated or coated with anti-progesterone monoclonal antibody (mAb) showed well-defined anodic responses for both species, with the more sensitive being 4-aminophenol. Scan rate studies produced evidence that surface mAb could impede the diffusion of 4-aminophenol, but not 1-naphthol, toward the electrode surface. This was supported by computer simulation for the electrochemical rate constant (khet) using 4-aminophenol, which gave values at uncoated and mAb-coated electrodes of 6.5 x 10(-4) and 3.0 x 10(-4) cm s-1, respectively. The applied potential for oxidation of 4-aminophenol was 230 mV lower than for 1-naphthol. Nevertheless, by operating below +400 mV versus a saturated calomel reference electrode, it was possible to obtain a chronoamperometric signal for 1-naphthol in the absence of electrochemical interference from milk. Using mAb-coated SPCEs, calibration curves were obtained for progesterone in oestrus whole cow's milk spiked with standard concentrations over the range 0-50 ng/ml, using either 4-APP or 1NP as enzyme substrate. Precision values for triplicate sensors were 5.3-18.3% for 4-APP and 4.1-12.4% for 1-NP. An assay of real whole milk samples from different cows at various stages of the oestrus cycle produced correlations against a commercial EIA of r = 0.840 and 0.946 for 4-APP and 1-NP, respectively, 1-NP possesses the advantages over 4-APP of being inexpensive, easy to obtain and soluble (1-naphthol cf. 4-aminophenol) at high pH. From these observations, it is concluded that 1-NP is the preferred substrate for use with our proposed milk progesterone biosensor.
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PMID:A comparison of 1-naphthyl phosphate and 4 aminophenyl phosphate as enzyme substrates for use with a screen-printed amperometric immunosensor for progesterone in cows' milk. 1045 17

Most of the double immunostaining protocols that have been introduced so far have been developed for application on fresh frozen material or based on different species antibodies. In liver tissue, general problems of double immunostaining techniques are further complicated by tissue-specific difficulties, such as necrosis or high intracellular protein content. To assess a reliable double immunostaining protocol for archived, paraffin embedded liver tissue, different protocols based on the use of same species primary antibodies were evaluated in terms of sensitivity, specificity and non-specific background staining in pathological liver specimens. We compared peroxidase-anti-peroxidase, alkaline phosphatase-anti-alkaline phosphatase (PAP/APAP), labelled-avidin-biotin (LAB/LAB) and digoxigenin-anti-digoxigenin (dig-a-dig/PAP) techniques using different cytokeratin antibodies and an antibody against PCNA. Comparison of the double immunostaining techniques revealed a high sensitivity and specificity in all procedures. Sections, which were stained employing PAP/APAP-technique, displayed a higher background staining compared to sections which were treated with the LAB/LAB or dig-a-dig/PAP protocol. In contrast to the dig-a-dig/PAP protocol, the LAB/LAB technique provides a better time/cost relationship. Therefore, we would like to recommend a modified LAB/LAB protocol for simultaneous detection of different antigens in archived liver tissue.
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PMID:Comparison of different double immunostaining protocols for paraffin embedded liver tissue. 1060 66

A new procedure is described to deposit paramagnetic beads on surfaces to form microscopic agglomerates. By using surface-modified beads, microscopic structures with defined biochemical activity are formed. The shape and size of agglomerates were characterized by scanning electron microscopy (SEM), and the biochemical activity was mapped with scanning electrochemical microscopy (SECM). This approach is demonstrated using beads modified with anti-mouse antibodies (Ab). After allowing them to react with a conjugate of mouse IgG and alkaline phosphatase (ALP), the beads were deposited as agglomerates of well-defined size and shape. The biochemical activity was recorded in the generation-collection SECM mode by oxidizing 4-aminophenol formed in the ALP-catalyzed hydrolysis of 4-aminophenyl phosphate at the surface of the beads. The signal height correlated with both the amount of beads present in one agglomerate and the proportion of Ab binding sites saturated with the ALP mouse IgG conjugate. The feedback mode of the SECM was used to image streptavidin-coated beads after reaction with biotinylated glucose oxidase.
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PMID:Spatially addressed deposition and imaging of biochemically active bead microstructures by scanning electrochemical microscopy. 1065 27

A bead based sandwich enzyme immunoassay coupled to electrochemical detection for ovalbumin has been developed. The enzyme label alkaline phosphatase was used to convert the substrate 4-aminophenyl phosphate to electroactive product 4-aminophenol. The detection was done in a microdrop by continuously monitoring the enzyme turnover with a rotating disk electrode. This reduces dilution of the enzyme product, a key to achieving low detection limits. The assay developed has a detection limit of 0.1 ng ml-1. Assay sensitivity in complex matrices such as food and serum was compared.
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PMID:Small volume bead assay for ovalbumin with electrochemical detection. 1128 35

The expression and regulation of alkaline phosphatase (AP) was studied in the human gastric cancer cell line TMK-1. Biochemical analysis, reverse transcription-polymerase chain reaction, and Northern blot analysis demonstrated that the cells express placental, germ cell, and intestinal AP isozymes constitutively. Dexamethasone (Dex), a synthetic glucocorticoid, was shown to specifically induce the placental AP activity to about 10-fold and sodium butyrate (NaBu) induced germ cell AP activity to about 4-fold, respectively. In contrast, these two agents showed little effect on the level of intestinal isozymes. Dex and NaBu also differentially induced the mRNA levels of the placental and germ cell APs. Northern blot analysis of the placental AP transcript in the presence of the transcription inhibitor, 5, 6-dichloro-1-beta-D-ribofuranosyl benzimidazole, revealed that the half-life of placental AP mRNA is about 27 h for both the Dex-treated and untreated cells. Nuclear run-on transcription analysis indicated an apparent increase in the rate of placental AP gene transcription in Dex-treated cells. These results indicated that the effect of Dex occurred primarily by activation of the placental AP gene transcription in the cells. In order to study the direct Dex and NaBu effect on AP gene expression, the proximal promoter regions of AP genes were fused to luciferase reporter vectors. Despite the high similarity in nucleotide sequences of these two genes, transient transfection analysis demonstrated that Dex and NaBu exerted a specific stimulation only through the respective placental and germ cell AP gene promoter. Taken together, this study indicates that the expression of PAP and GCAP isozymes have specific regulatory mechanisms that can be differentially controlled by signals including glucocorticoid and NaBu.
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PMID:Differential regulation of placental and germ cell alkaline phosphatases by glucocorticoid and sodium butyrate in human gastric carcinoma cell line TMK-1. 1136 Nov 39

A microfluidic device for conducting electrochemical enzyme immunoassays is described. The new "lab-on-a-chip" protocol integrates precolumn reactions of alkaline phosphatase-labeled antibody (anti-mouse IgG) with the antigen (mouse IgG), followed by electrophoretic separation of the free antibody and antibody-antigen complex. The separation is followed by a postcolumn reaction of the enzyme tracer with the 4-aminophenyl phosphate substrate and a downstream amperometric detection of the liberated 4-aminophenol product Factors influencing the reaction, separation, and detection processes were optimized, and the analytical performance was characterized. An applied field strength of 256 V/cm results in free antibody and antibody-antigen complex migration times of 125 and 340 s, respectively. A remarkably low detection limit of 2.5 x 10(-16) g/mL (1.7 x 10(-18) M) is obtained for the mouse IgG model analyte. Such combination of a complete integrated immunoassay, an attractive analytical performance, and the distinct miniaturization/portability advantages of electrochemical microsystems offers considerable promise for designing self-contained and disposable chips for decentralized clinical diagnostics or on-site environmental testing.
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PMID:Electrochemical enzyme immunoassays on microchip platforms. 1172 36


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