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)

L-p-bromotetramisole was used to inhibit non-intestinal alkaline phosphatase (of liver or bone origin) (EC 3.1.3.1; ALP) in plasma, and intestinal ALP was measured from the uninhibited activity. The method of determination is convenient and correlated well with measurement by immunocapture assay. If carried out in parallel with wheat-germ lectin precipitation of bone ALP, subtraction of intestinal ALP activity from that of non-bone ALP in the supernatant can be used to measure the ALP that originates from the liver in men and non-pregnant women.
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PMID:Measurement of alkaline phosphatase of intestinal origin in plasma by p-bromotetramisole inhibition. 201 25

In order to elucidate the cell characteristics of head and neck squamous cell carcinomas, the cell kinetics and lectin binding patterns were compared with the histological classification and staging of the tumors, using surgically resected materials (maxillary sinus 10, oral cavity 21, pharynx 8, larynx 11). Eight biotinylated lectins (WGA, 1-PHA, ConA, UEA1, RCA1, SBA, DBA, PNA) were applied to the paraffin-embedded sections, and were visualized histochemically by the streptavidin-alkaline phosphatase method. The DNA contents of the isolated carcinoma cells obtained from the adjacent thick sections were evaluated using an epi-illumination cytofluorometer after propidium iodide staining. On lectin histochemistry, the binding pattern of WGA lectin was similar between carcinoma tissues and normal tissues, but the binding was more intense in well differentiated than less differentiated carcinomas. Lymph node metastasis was found to be related to the presence of cells with poor WGA-binding. In the binding patterns of the other lectins, RCA1, SBA and ConA were related to the differentiation of carcinomas, but they were not related to the TNM-classification. DNA cytofluorometry exhibited marked polyploidization, which progressed with the advancement of the clinical and pathological staging of carcinomas. However, the DNA ploidy pattern was not associated with the cell characteristics such as the degree of histological differentiation and the lectin-binding pattern, except that the appearance of aneuploidy had some relationship with the binding-patterns of UEA1 and 1-PHA.
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PMID:[Lectin-binding patterns and cell kinetics of head and neck squamous cell carcinomas]. 201 15

The authors describe an unusual variant of alkaline phosphatase (ALP) discovered in a patient with a 90-fold increase in serum ALP. The variant ALP was indistinguishable from the bone isoenzyme when subjected to chemical inhibition, heat inactivation, lectin precipitation, and routine electrophoresis. However, treatment with neuraminidase produced a marked decrease in the ALP variant's electrophoretic mobility and a reduction in its molecular weight. A bone marrow biopsy revealed metastatic infiltration of the bone marrow by adenocarcinoma of the prostate accompanied by a remarkable amount of new bone formation, suggesting a bone origin for the unusual isoenzyme. The authors believe this to be the first report of an ALP variant with these properties.
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PMID:A unique bone-like variant of alkaline phosphatase. 202 30

A procedure is proposed for the separation of multiple forms of 5'-nucleotidase (EC 3.1.3.5) by cellulose acetate electrophoresis. The effects of various treatments (wheat-germ lectin, neuraminidase, n-butanol, papain, Triton X-100 and precipitation of LDL and VLDL) on the electrophoretic pattern of 5'-nucleotidase and alkaline phosphatase were studied. In healthy controls, the presence of three fractions with alpha 1, alpha 2 and beta mobilities was observed, the latter being the major one. In different hepatobiliary diseases a close relationship between the presence of high molecular weight alkaline phosphatase and the increase in the ratio Total/beta 5'-nucleotidase was observed, showing that the increase in total 5'-nucleotidase in these patients is mainly due to the alpha 1 isoform. The nature of these forms is discussed.
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PMID:Electrophoretic separation of 5'-nucleotidase multiple forms. 204 89

Serum levels of osteocalcin (S-OC) and lectin-precipitable alkaline phosphatase activity (S-LAP) are sensitive markers of osteoblastic activity. Diurnal variation has been found for S-OC but has not been reported for S-LAP. We measured S-LAP and serum total alkaline phosphatase (S-TAP) in samples drawn every 60 min during a 24-h study period in nine normal subjects and correlated the findings with the diurnal variation in S-OC. A significant (p less than 0.05) diurnal variation in S-LAP characterized by peaks at 1430 hours and 2330 hours and nadir at 0630 hours was found. Peak levels were 30% higher than nadir level (p less than 0.05). S-TAP also varied significantly (p less than 0.05) with nadir at 0630 hours, showing a difference of 23% between peak and nadir levels (p less than 0.05). Significant cross-correlation was found between S-OC and S-LAP and S-TAP when these lagged 4 h after S-OC: r = 0.51 (p less than 0.02) and r = 0.65 (p less than 0.003), respectively. In other words, changes in S-LAP and S-TAP preceded changes in S-OC by 4 h. There were no significant cross-correlations between the non-lectin-precipitable fraction of AP and S-OC. In conclusion, S-LAP varies in a diurnal rhythm closely related with the diurnal rhythm of S-OC. The almost similar patterns in the diurnal serum levels of these two osteoblastic products strongly suggest that osteoblastic activity fluctuates rhythmically during the day in humans.
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PMID:Diurnal rhythm in serum activity of wheat-germ lectin-precipitable alkaline phosphatase: temporal relationships with the diurnal rhythm of serum osteocalcin. 208 22

The acute toxicity of lectin ML I from the toxic drug, mistletoe, was demonstrated in previous experiments. Because the reason for this extremely high toxicity is not yet clear, mice were studied histochemically at different times after treatment with various doses of ML I, ML I A or ML I B chain separately, or recombinations of ML I A and ML I B. Various plasma membrane-associated hydrolases as well as Golgi apparatus-and endoplasmic reticulum-linked hydrolases, peroxisomal and extraperoxisomal oxidases, lysosomal hydrolases, mitochondrial dehydrogenases, the cytoskeletal proteins keratin and vimentin as well as iron, glycogen and lipids were analysed in all organs and tissues of female mice. Irrespective of the dose, a clear-cut response was only observed in the liver. After ML I treatment, glycogen disappeared completely from all hepatocytes, and this effect did not depend on the ML I-concentration and exposure time. The increase in activity of Golgi-associated thiamine pyrophosphatase in hepatocytes and of non-specific alkaline phosphatase in the sinusoidal endothelial cells depended on the applied ML I concentration and the time of treatment. Doses of 600 or 900 ng ML I/kg drastically increased the phosphatase activities. These clear-cut changes of glycogen and enzyme activities were not observed after administration of the ML I B chain alone, and less so when the mice were treated only with the ML I A chain, or were treated with a recombination of ML I A and ML I B even at concentrations higher than that of ML I.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Histochemical response of mice to mistletoe lectin I (ML I). 228 17

To separate liver and bone alkaline phosphatase (ALP) isoenzymes in human serum, we used high-performance affinity chromatography (HPAC) on a column of wheat-germ lectin conjugated to 7-microns-diameter silica particles and an eluent containing N-acetyl-D-glucosamine (NAG). On-line spectrophotometric detection of ALP involved pumping diethanolamine-buffered p-nitrophenyl phosphate solution post-column. Bone and liver isoenzymes could be separated into two peaks with only 10% overlap when an exponential gradient was used. A linear-step gradient separated 80.9% of liver ALP and 91.6% of bone ALP in two distinct peaks. True bone and liver ALP peak areas for the linear-step gradient were determined by using correction factors, because each peak contained a co-eluted portion of the other ALP isoenzyme. The detection limit improved 10-fold over those of other techniques for ALP isoenzymes, owing to the relatively large sample that could be applied to the column. Correlation with a urea-inactivation procedure was reasonable for patients' serum samples (r = 0.98 and 0.79 for liver ALP and bone ALP, respectively).
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PMID:Liver- and bone-derived isoenzymes of alkaline phosphatase in serum as determined by high-performance affinity chromatography. 230 67

The placental alkaline phosphatase was purified by immunoaffinity chromatography from ovarian epithelial tumours to homogeneity. Up to 40% of the catalytical phosphatase activity in these tumours was derived from this placental type alkaline phosphatase (PLAP). The purified enzyme were similar to those of PLAP, whereas the PLAP-like isozyme was more heat-stable and resistant to 8 M urea than PLAP. The amino terminal sequence of the PLAP-like enzyme demonstrated heterogeneity at position three in the N-terminal end compared with PLAP. Phenyl-Sepharose affinity chromatography and different lectin chromatographies demonstrated the tumour-derived enzyme to be microheterogeneous, both with regard to concanavalin A binding and hydrophobicity properties.
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PMID:Purification and characterisation of the placental-like alkaline phosphatase from ovarian epithelial tumours. 238 81

The binding of PSA, PNA, HPA, WGA, Con A, LCL, RCA, SBA, and PHA lectins to epithelial structures of the normal rabbit appendix was studied. Differences were observed in the affinity of some lectins to the epithelium of the intercryptal lining of the rabbit appendix, to the epithelium hemming the glandules and crypts of the domes of Peyer's patches. The obtained results document the difference in the affinity of individual batches of anti-WGA antibodies to this lectin after its binding to the epithelial structures studied. This implies the possibility that differently reacting antibodies may develop to different commercially available batches of WGA. Precipitation of WGA at sites of alkaline phosphatase occurrence demonstrates the relationship of this enzyme to WGA binding sites in tissues.
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PMID:[Lectin histochemical analysis of the epithelial lining of the appendix in rabbits]. 239 27

A sensitive immunoenzymatic double-staining technique is presented for the simultaneous visualization of lectin-binding sites and antigenic structures detected by monoclonal antibodies. The lectin is demonstrated by an extended unlabeled peroxidase-antiperoxidase (PAP) technique and the monoclonal antibody by an alkaline phosphatase-antialkaline phosphatase (APAAP) method, which corresponds to the standard PAP technique. 3-amino-9-ethylcarbazole (AEC) and fast blue BB salt serve as substrates for the peroxidase and the alkaline phosphatase, respectively. The antisera and the enzyme complexes raised in different animals enable the performance of three parallel incubation steps. The staining procedure requires three and a half hours altogether. This method proved to be highly discriminative and rather insensitive to interference by various artifacts.
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PMID:Simultaneous demonstration of lectin-binding sites and antigens detected by monoclonal antibodies in a parallelized double-staining technique: a highly discriminative and quickly developing technique for frozen sections. 241 93


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