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)

We investigated the prevalence and characteristics of intestinal alkaline phosphatase (ALP; EC 3.1.3.1) identified in human serum by cellulose acetate electrophoresis in 8% of fasting serum samples from hospital patients (n = 500) and in 35% of fasting serum samples from patients with diabetes mellitus (n = 106; not differentiated between types 1 and 2). The intestinal ALP electrophoretic band was usually heterogeneous and contained two major subtypes of ALP. Isoelectric focusing of intestinal-ALP-positive serum treated with levamisole and neuraminidase (EC 3.2.1.18) revealed two distinct regions of enzymatic activity that comigrated with ALP extracted from small intestinal and colonic mucosa. Anodic intestinal ALP was resistant to treatment with levamisole and neuraminidase and comigrated with ALP from small intestinal mucosa. The more-cathodic intestinal ALP, which comigrated with ALP from colonic mucosa, was completely inhibited by levamisole and converted by neuraminidase to a species with a more basic pI than that of neuraminidase-digested tissue-nonspecific form. This component of intestinal ALP may be of vascular origin.
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PMID:Prevalence and properties of the intestinal alkaline phosphatase identified in serum by cellulose acetate electrophoresis. 156 15

We investigated by enzyme electrophoresis after prolonged neuraminidase treatment the activity of "intestinal variant" (alpha 2-globulin mobility) alkaline phosphatase (EC 3.1.3.1; ALP) in the plasma of 189 patients selected for disorders (diabetes mellitus, liver cirrhosis, and chronic renal failure) with a known high frequency of increased plasma intestinal (beta-globulin mobility) ALP activity. The overall frequency of the variant ALP was 23.8%, whereas in the samples showing intestinal ALP it was 45.0%. The variant ALP was not observed in the absence of intestinal ALP, nor in patients of blood group A. Its frequency did not differ significantly between the different patient groups. Quantification of the variant ALP by densitometry was unsatisfactory but the quantity could be estimated by subtracting the intestinal ALP activity measured by electrophoresis from the activity determined by immunoassay with monoclonal antibody that reacts with both the intestinal and the variant forms. This indicated median activity of 12 U/L for the variant, approximately equal to that of the concomitant intestinal ALP. From the effects of papain and bromelain treatments, we suggest that "intestinal variant" represents intestinal ALP with attached membrane-binding domain.
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PMID:Intestinal variant alkaline phosphatase in plasma in disease. 170 Jul 41

Surface charge of Leishmania mexicana amazonensis was investigated by direct zeta-potential determination and ultrastructural cytochemistry, and its surface tension was studied by measurements of the advancing contact angle formed by the parasite monolayers with drops of liquids of different polarities. Both virulent and avirulent promastigotes exhibited negatively charged surfaces with a zeta-potential of about -15 mV. Treatment of these cells with trypsin, alkaline phosphatase, or phospholipase C rendered their surfaces less negatively charged, whereas neuraminidase did not alter the parasite negativeness. Cytochemically, we could observe a reduction in the cationized ferritin binding after the parasite treatment with each of the former enzymes, but not with neuraminidase. The surface free energy of parasites was calculated by taken to account the London dispersion, the Keeson dipole-dipole, and the Debye dipole-induced forces, as well as the surface polarity of the parasites and their zeta-potentials, by considering their adhesion to polystyrene surfaces. The delta G values of -6.4 and -18.1 mJ.m-2 were obtained for avirulent and virulent promstigotes, respectively.
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PMID:The surface free energy of Leishmania mexicana amazonensis. 170 80

We showed previously that human thyroglobulin (hTG) contains anionic complex carbohydrate units with up to four sulfate groups, some containing both sulfate and sialic acid. Recent reports indicate that the carbohydrate units of hTG may also contain phosphate, but these reports are not all in accord. The purpose of this study was to confirm the presence of phosphate on the carbohydrate units of hTG and to determine whether phosphate coexists with other acidic moieties, such as sulfate and sialic acid, on the same carbohydrate units. Alkaline phosphatase and acid hydrolysis were used to detect phosphate on the sulfated carbohydrate units of hTG derived from normal and neoplastic tissues. Thyroid fragments from two patients were incubated for 16 h in [35S]sulfate-containing medium, and hTG was purified. Complex carbohydrates were released from hTG with endoglycosidase-F and analyzed at pH 2.2 on a HPLC ion exchange column. Sulfate-containing peaks were monitored by radioactivity, and sialic acid-containing ones were identified by their reduced charge after neuraminidase or acid treatment. None of the sulfate-labeled carbohydrate peaks shifted after alkaline phosphatase treatment alone, indicating that none of them contained phosphomonoesters. Several of the sulfate-labeled peaks shifted after acid hydrolysis, some to positions of decreased charge, due to removal of sialic acid, and some to positions of increased charge, suggesting the presence of phosphodiesters. The latter was confirmed by the observation that some of the newly formed peaks were susceptible to alkaline phosphatase digestion. Thus, acid hydrolysis converted phosphodiesters into alkaline phosphatase-susceptible phosphomonoesters, most likely mannose-6-phosphate. We conclude that some anionic complex carbohydrate units of hTG contain exclusively sulfate, while others contain combinations of sulfate, sialic acid, and phosphodiesters. Phosphodiesters are present in the sulfated carbohydrate units of hTG from normal as well as neoplastic thyroid tissue.
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PMID:Anionic carbohydrate groups of human thyroglobulin containing both phosphate and sulfate. 185 82

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

Changes of the three types, termed here as alpha, beta and gamma, in the secretory functions present in the submandibular glands (SMG) of male rats were observed throughout almost all animal lives from 2 weeks to 24 months of age, by measuring changes of the wet weights of the SMG, salivary volumes secreted, the concentrations of protein, calcium and inorganic phosphate, and the types of proteins secreted in response to alpha-methylnoradrenaline (alpha-mNA) for the alpha-type, isoproterenol (IPR) for the beta-type and clonidine (Clonid) for the gamma-type, volumetrically, colorimetrically, atomic absorption-pectrophotometrically and isoelectric focusing electrophoretically. The molecular weight, isoelectric point and some posttranslational variations of a purified protein were elucidated by SDS-polyacrylamide gel electrophoresis (PhastSystem), isoelectric focusing electrophoresis (IEF, PhastSystem) on gradient pH 3.5 to 5 gels and neuraminidase or alkaline phosphatase treatment. The localization in the SMG, the inhibitory effects on the BrdU incorporation of the cultured thymocytes and the adhesive properties to the acrylic resin plate of this antigen were also analyzed by the indirect immunofluorescence, IEF and protein detection methods. The wet weights of the SMG were substantially increased up to 3.5 months of age with a positive correlation to body weight, but thereafter it reached the plateau level up to 24 months of age, somewhat different from changes of body weight. The salivary volumes as well as the amounts of protein secreted in response to alpha-mNA, IPR and Clonid were positively correlated to the wet weights of the SMG throughout the animal life. The concentration of calcium in the three types of secretions was positively correlated to the protein concentration, whereas the concentration of inorganic phosphate was tended to be reversely correlated to the salivary flow rate with some exceptions throughout the animal life. The gamma-type of proteins was not greatly changed, whereas the alpha- and beta-types of proteins were greatly changed in some proteins quantitatively or qualitatively throughout the animal life.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:[Changes of three types in the secretory systems present in the rat submandibular glands during aging]. 213 43

Electron microscopic observations showed that the fungal metabolite brefeldin A caused disassembly of the Golgi complex in human choriocarcinoma cells and accumulation of alkaline phosphatase (ALP) in the endoplasmic reticulum (ER) and nuclear envelope, where ALP was not apparently detectable in control cells. Pulse/chase experiments with [35S]methionine demonstrated that in the control cells, ALP synthesized as a 63-kDa precursor form was rapidly converted to a 66-kDa form, by processing of its N-linked oligosaccharides from the high-mannose type to the complex type, which was expressed on the cell surface after 30 min of chase. In contrast, in the brefeldin-A-treated cells the precursor was gradually converted to a 65-kDa form, slightly smaller than the control mature form, which was not expressed on the cell surface even after a prolonged time of chase. Kinetics of the ALP processing in the brefeldin-A-treated cells demonstrated that the precursor was initially converted to an intermediate form, partially sensitive to endo-beta-N-acetylglucosaminidase H (endo H), then to an endo-H-resistant 65-kDa form. In addition, this form was found to be sensitive to neuraminidase digestion, though its sialylation was not so complete as that of the control mature form. Taken together, these results suggest that under disassembly of the Golgi complex caused by brefeldin A, oligosaccharide-processing enzymes including sialyltransferase, an enzyme in the trans Golgi cisterna(e) and/or the trans Golgi network, might be redistributed into the ER and involved in processing of the oligosaccharides of ALP accumulating there.
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PMID:Intracellular accumulation and oligosaccharide processing of alkaline phosphatase under disassembly of the Golgi complex caused by brefeldin A. 226 2

Investigation of mild, inherited increased serum alkaline phosphatase activity partially combined with Gilbert's syndrome in one family showed, apart from a normal liver fraction, an intestinal isoenzyme pattern and an extra band in the agar electrophoresis. Analysis by agarose electrophoresis before and after incubation of neuraminidase showed that the extra fraction was an intestinal variant isoenzyme. The precise genetic background of the two disorders in this family could not be determined from the available data. Abnormal activities of (regular) intestinal alkaline phosphatase isoenzyme caused the increase in serum alkaline phosphatase in the absence of disease.
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PMID:Familial increased serum intestinal alkaline phosphatase: a new variant associated with Gilbert's syndrome. 231 88

Intestinal and serum leucine aminopeptidase (LAP) and alkaline phosphatase (AKP) were characterized by electrophoresis for eight inbred strains of laboratory mice. Intestinal LAP and AKP of adult mice were expressed concordantly within strains, as banded or diffuse, and concordantly for rate of migration within strains that had diffuse isozymes. All strains, except DD/S, had a single band of serum LAP and a single, diffuse zone of serum AKP. DD/S had a double band of serum LAP as well as isozymes of intestinal LAP and AKP unlike those of other strains. All strains displayed similar, neuraminidase-sensitive isozymes of intestinal LAP and of AKP prior to weaning, but after weaning there was marked sensitivity to neuraminidase only in DD/S. In interstrain crosses, banded/diffuse, migration rate, and neuraminidase sensitivity were inherited as independent autosomal traits, with indications of variable penetrance and genetic interaction.
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PMID:Intestinal leucine aminopeptidase and alkaline phosphatase: genetic regulation and development in mice. 239 81


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