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)

Plasma membrane proteins and glycoproteins have been isolated from Chinese hamster cells of the spontaneously transformed DC-3F parental cell line and the DC-3F/AD X line with a high level of acquired resistance to actinomycin D. Plasma membrane preparations from both cell lines band at 1.16 g/ml after isopycnic centrifugation. We present evidence to indicate differences in the leucylpeptide backbones of the antibiotic-sensitive cells and the drug-resistant DC-3F/AD X cells. In addition, there are differences in the plasma membrane glycopeptides of the two cell lines as revealed by sodium dodecyl gel electrophoresis. Drug-resistant cells synthesize a surface glycopeptide which is much larger than the major one present on the drug-sensitive cells. Both of these cell lines are devoid of 5'-nucleotidase and alkaline phosphatase activities. The role of plasma membrane protein differences in drug-resistant cells is discussed.
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PMID:Plasma membrane proteins and glycoproteins from Chinese hamster cells sensitive and resistant to actinomycin D. 74 79

Insulin receptor characteristics were examined in purified brush border membrane from the syncytiotrophoblast of the normal human placenta and quantified during membrane preparation. Insulin receptor concentration was enriched 10- to 15-fold in this preparation, and insulin receptor specific activity followed closely the enrichment values for microvillus plasma membrane markers, alkaline phosphatase, Ca2+- and Mg2+-ATPase, and 5'-nucleotidase during cell fractionation. Insulin receptor concentrations and marker enzyme analyses were compared in whole homogenate, mitochondrial, microsomal, and microvillus fractions, and these fractions were characterized by SDS-gel electrophoresis. Microvillus insulin receptor interactions were dependent on time, [125I]iodoinsulin concentration, protein, and unlabeled hormone concentrations. Competition studies with porcine insulin and [125I]iodoinsulin for this receptor revealed a curvilinear Scatchard plot. Insulinase was demonstrated at 37 C but was minimal at 24 C in the microvillus fraction. Electron microscopy of the microvillus membrane preparation revealed its composition to be mainly spherical closed membrane vesicles and brush border fragments. Sodium dodecyl sulfate polyacrylamide and isoelectric focusing gels of membrane fractions were compared. Actin was tentatively identified as a major microvillus membrane protein and was further fractionated: beta-Actin and gamma-actin were present in approximately equal concentrations. The localization of the insulin receptor in the microvillus brush border of the human placenta suggests that this receptor interacts with maternal, rather than fetal insulin.
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PMID:Characteristics of the microvillus brush border of human placenta: insulin receptor localization in brush border membranes. 75 22

Methods have been developed for the isolation on a semi-micro scale of a plasma membrane-enriched fraction from rat islets of Langerhans. An important feature of these experiments is the use of 125I-labeled wheat germ agglutinin as a specific probe for plasma membrane-containing fractions. The partly purified plasma membrane fraction had a density in sucrose of about 1.10 and was enriched in the activities of 5'-nucleotidase, alkaline phosphatase, sodium-potassium, and magnesium-dependent ATPase and adenylate cyclase. It contained only very low levels of acid phosphatase, cytochrome c oxidase, insulin, and RNA. Further purification was hampered by the relatively small amounts of fresh plasma membrane material that could be obtained from 16-24 rats in each experiment. When islets were prelabeled with radioactive fucose, the plasma membrane-enriched fraction contained radioactivity at a four- to fivefold higher specific acivity than the whole islet homogenate. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis of plasma membrane-enriched fractions pooled from several experiments revealed a distinctive pattern of protein bands as compared with other less pure fractions. With respect to rapidity, apparent specificity, and easy reversibility of the labeling of the plasma membrane fraction, 125I-wheat germ agglutinin provides a highly useful tool for the detection of microgram quantities of plasma membrane components which should be applicable to many other systems as well.
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PMID:Preparation and characterization of plasma membrane-enriched fractions from rat pancreatic islets. 79 56

Reports on correlations between the activity of so-called "marker enzymes of cholestasis" in serum and the ultrastructural changes of the liver are rare. Therefore studies of ultrastructural changes were carried out in 40 patients with intrahepatic cholestasis. In the patients' serum activity of alkaline phosphatase, bile duct alkaline phosphatase, leucine-aminopeptidase (LAP), and 5'-nucleotidase (5'-Nu) as well as the concentration of bilirubin were determined. The results showed a significant correlation between the morphometry of the bile canaliculi and the serum activity of LAP and 5'-Nu. In patients with elevated LAP, an enlargement of the bile canaliculi could be proved. An increased serum activity of 5'-Nu correlated with a higher incidence of bile canaliculi in the ultrastructural picture. The results suggest an investigation of the ultrastructure of bile canaliculi and the determination of marker enzymes of cholestasis in the serum may both contribute to the assessment of cholestatic liver disease.
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PMID:[Ultrastructural-morphometric analysis of liver biopsies in patients with intrahepatic cholestasis. I. Correlations between morphometry of bile canaliculi and so-called "marker enzymes of cholestasis" (author's transl)]. 80 5

Two subfractions of bovine thyroid plasma membranes, light membranes (L-membranes) and heavy membranes (H-membranes), were obtained by a discontinuous sucrose gradient centrifugation of plasma membranes. Electron microscopy of the plasma membrane and its subfractions showed that the H-membranes were very similar to the plasma membrane fraction, both contained junctional complexes, long membrane sheets, and vesicles. In contrast, the L-membranes consisted mainly of short membrane sheets and vesicles, and only a few junctional complexes. The H-membranes had greater adenylate cyclase activity which responded to thyroid-stimulating hormone (TSH) while this hormone had very little effect on the enzyme activity in the L-membranes. Despite the marked difference in TSH stimulation of adenylate cyclase activity in the H- and L-membrane fractions, specific binding of 125I-TSH was similar in both fractions. The L-membranes had higher specific activities of 5'-nucleotidase and Mg2+ATPase while (Na+ + K+)-ATPase and alkaline phosphatase activities were similar in the two subfractions. Protein kinase activity of H-membranes was not significantly stimulated by exogenous cyclic adenosine 3':5'-monophosphate (cAMP). Plasma membranes and H-membranes contained a substrate capable of being phosphorylated. Such phosphorylation was slightly increased by addition of soluble protein kinase. The phosphorylation of exogenous histone by protein kinase of plasma membranes and H-membranes was augmented by cAMP. In contrast, L-membranes had very little protein kinase activity even when exogenous histone was added. They were not a very good substrate for cytosolic protein kinase.
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PMID:Preparation and characterization of subfractions of bovine thyroid plasma membranes. 85 12

In the present attempt, kidney from newly born albino-rat litters has been examined for few enzymes. Those selected for the study include, alkaline phosphatase, acid phosphatase; adenosine monophosphatase, nonspecific osterase and leucine amino peptidase. All the enzymes were observed exhibiting strong positive reactions except moderate acid phosphatase. Furthermore, a comparison of relative enzyme activities with adult rat kidney has been made. Variations in the distribution and intensity of reactions this observed have been discussed in relation to the hypothesis that redistribution of enzymes occurs as the animal becomes older. Functional role of these enzymes in the young kidney have also been discussed.
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PMID:Postnatal enzymorphology of the albino-rat kidney. 86 15

Human erythrocyte ghosts were solubilized in a low ionic strength medium containing 1% Triton X-100 and subjected to electrophoresis in polyacrylamide gels containing Triton X-100. Five major bands were stained with Coomassie Blue, all except one band being heterogenous when re-electrophoresed in gels containing sodium dodecyl sulphate. It was possible to detect acetylcholinesterase, non-specific esterase, ATPase, alkaline phosphatase, 5'-nucleotidase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, and aldolase activities on the Triton-containing polyacrylamide gels. Two of the enzymes, ATPase and 5'-nucleotidase, showed substantial inhibition by Triton X-100 in quantitative studies. This appears to be a useful method for studying membrane enzymes in normal and pathological red cells.
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PMID:Polyacrylamide gel electrophoresis of human erythrocyte membrane enzymes solubilized with triton X-100. 89 Sep 65

Concanavalin A inhibits serum 5'-nucleotidase activity, without causing significant inhibition of alkaline phosphatase activity. This observation serves as the basis for a new method for assaying the 5'-nucleotidase activity in serum, which depends upon the difference between the enzymic hydrolysis of adenosine-5'-monophosphate in the presence and absence of concanavalin A. A denosine released by the 5'-nucleotidase reaction is deaminated by a coupled reaction with adenosine deaminase to liberate inosine and ammonia, and ammonia is measured colorimetrically by the Berthelot reaction. In sera from 40 healthy adult persons, 5'-nucleotidase activity averaged 6.4 U/liter (SD, +/-2.0; range, 3-12). In sera from 100 patients, measurements of 5'-nucleotidase activity by the new assay averaged 8% lower than by a generally accepted method in which phenyl phosphate is used to suppress hydrolysis of adenosine-5'-monophosphate by alkaline phosphatase activity. The clinical validy of the new assay was tested by measuring serum 5'-nucleotidase activities in rats with bile duct ligation and in rats treated with thioacetamide to induce hepatocellular injury.
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PMID:Inhibition by concanavalin A as the basis for a specific assay of serum 5'-nucleotidase activity. 92 81

Human duodenal fluid, secretion fluid of a villous adenoma of the rectum, urine and culture medium of HeLa cells contain plasma membrane fragments which can be revealed by electrophoresis in different media, gel filtration on Sepharose 4-B, electron microscopy and cytochemistry. They carry plasma membrane enzymes (alkaline phosphatase EC 3.1.3.1, leucine aminopeptidase EC 3.4.1.1, 5'-nucleotidase EC 3.1.3.5, maltase EC 3.2.1.20) in the same ratio as the membranes of the cells of origin. Equilibrium density centrifugation results in recovery of these plasma membrane fragments at density 1.190 (g/ml) in CsCl, 1.165 (g/ml) in sucrose, and 1.135 (g/ml) in metrizamide. Similar plasma membrane fragments were decribed previously in the serum of certain liver patients. These observations give evidence that shedding of whole plasma membrane fragments (koinozymic shedding) is a widespread feature of viable cells.
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PMID:Spontaneous shedding of plasma membrane fragments by human cells in vivo and in vitro. 92 96

Sodium butyrate causes HeLa cells to assume an elongated and jagged shape. Ultrastructurally this change is associated with the formation of bundles of microfilaments. Desmosomes were present between adjacent cells. No increase in microtubules was observed in the butyrate-treated cells. Butyrate induces an increase in the activity of 2 membrane-bound enzymes, alkaline phosphatase and 5'-nucleotidase; however, the activity of a third membrane enzyme, acetylcholine esterase, is reduced. The activities of the several other enzymes with different subcellular localizations are not significantly increased. Colcemid and cytochalasin B prevent or reverse the butyrate-mediated change in HeLa cell morphology and also partially inhibit the induction of alkaline phosphatase activity in these cells. The effect of cytochalasin B on alkaline phosphatase induction may be caused by a reduction in protein synthesis produced by this fungal metabolite.
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PMID:Ultrastructural and enzymic modulation of HeLa cells induced by sodium butyrate and the effects of cytochalasin B and colcemid. 97 76


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