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)

Ferritin-conjugated specific antibodies have been used to localize beta-galactosidase and both the monomer and active dimer of alkaline phosphatase in frozen thin sections of cells of Escherichia coli O8 strain F515. The even distribution of the ferritin marker throughout cells that had been induced for beta-galactosidase synthesis, frozen, sectioned, and exposed to ferritin-anti-beta-galactosidase conjugate showed that this enzyme was present throughout the cytoplasm of these cells. Frozen thin sections of cells that had been derepressed for the synthesis of alkaline phosphatase were exposed to both ferritin-anti-alkaline phosphatase monomer and ferritin-anti-alkaline phosphatase dimer conjugates, and the ferritin markers showed a peripheral distribution of both the monomer and the dimer of this enzyme. This indicates that alkaline phosphatase is present only in the peripheral regions of the cell and argues against the existence of a cytoplasmic pool of inactive monomers of this enzyme. This peripheral location of both the monomers and dimers of alkaline phosphatase supports the developing concensus that this enzyme is, like other wall-associated enzymes, synthesized in association with the cytoplasmic membrane and vectorially transported to the periplasmic area, where it assumes its tertiary and quaternary structure and acquires its enzymatic activity.
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PMID:Immunocytological investigation of protein synthesis in Escherichia coli. 32 33

Seminomas and control tissues were analyzed for several tumor markers. Very high levels of placental alkaline phosphatase (PLAP)-like enzyme levels were found in all 18 seminomas studied. The majority of the seminomas were of phenotype I, thus differing from palcental PLAP. The mean amount of enzyme protein as measured by monoclonal antibodies, was 100 times higher than in non-malignant tissues and 10 times lower than in placental tissue. The specific enzymatic activity in seminomas was about half of that observed in placenta. Similarly, the specific activity of PLAP-like enzymes in sera of patients with seminoma was only about half of that found in pregnancy sera. HCG was strongly elevated in 3 seminomas, but not obviously related to PLAP. Thirteen of the 17 pure seminomas had HCG over 100 IU/g, which was not seen in normal testes. Liver alkaline phosphatase (LAP) and intestinal alkaline phosphatase (IAP) were high in seminomatous tissues, the mean increases being 60-fold and 20-fold, respectively. The highest IAP levels were found in 2 yolk-sac tumors. Ferritin was moderately elevated in seminomas, but high in several control tissues. Carcinoembryonic antigen (CEA) was not elevated and alpha-fetoprotein (AFP) was not detected at all in pure seminomas. A decrease in carbohydrate antigen 50 (CA-50) content was noted in seminomas as compared to normal testes, yolk-sac tumors and choriocarcinomas. Defects in tumor-related enzymes may account for increase of PLAP and decrease of CA-50.
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PMID:Patterns of seminoma tissue markers and deletions. 244

This study surveys the extent and severity of haematological and biochemical abnormalities which occurred in 265 patients with pulmonary tuberculosis, and records the haematological changes that occur with treatment. Anaemia was present in 60 per cent of patients, more frequently in males than in females. Leucocytosis with neutrophilia occurred in 40 per cent, lymphopenia in 17 per cent and monocytopenia in 50 per cent. Platelet count and erythrocyte sedimentation rate were elevated in 52 and 80 per cent respectively. Bone marrow aspiration and trephine biopsy were of limited diagnostic value. Ferritin and vitamin B12 levels were increased in 94 and 57 per cent of subjects respectively whilst serum and red cell folic acid were within normal limits in 83 per cent. The frequency of the important biochemical changes were hyponatraemia (43 per cent) and hypoalbuminaemia (72 per cent); alkaline phosphatase, aspartic transaminase and lactic dehydrogenase levels were elevated in approximately a third of patients possibly due to unsuspected dissemination. There was a close correlation between the acid-fast bacilli in sputum and abnormal values, particularly those of body weight, haemoglobin, platelet count, white cell count and erythrocyte sedimentation rate. Failure of these indices to return to normal was invariably associated with persistent excretion of acid-fast bacilli. We have shown that haematological and biochemical abnormalities in pulmonary tuberculosis are common and may be valuable aids to diagnosis. Some haematological markers also reflect response to treatment.
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PMID:The haematological and biochemical changes in severe pulmonary tuberculosis. 261 37

In Reuber rat hepatoma cells (R-Y121B), alkaline phosphatase activity increased without de novo enzyme synthesis (Sorimachi, K., and Yasumura, Y. (1986) Biochim. Biophys. Acta 885, 272-281). The enzyme was partially purified by butanol extraction from the particulate fractions. The incubation of the extracted alkaline phosphatase with the cytosol fraction induced a large increase in enzyme activity (5-10-fold of control). The dialyzed cytosol was more effective than the undialyzed cytosol during an early period of incubation at 37 degrees C. This difference between the dialyzed and the undialyzed cytosol fractions was due to endogenous Na+. For maximal activation of the enzyme, both Mg2+ above 1 mM and Zn2+ at low concentrations (below 0.01 mM) were needed, although Zn2+ at high concentrations (above 0.1 mM) showed an inhibitory effect. Zn2+ and Mg2+ alone slightly increased alkaline phosphatase activity. This activation of the enzyme was temperature dependent and was not observed at 0 or 4 degrees C. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate showed that the increase in alkaline phosphatase activity did not involve the fragmentation of the enzyme and that 65Zn2+ bound to it during enzyme activation with 65Zn2+ and Mg2+. The cytosol fraction not only supplied Zn2+ to the nascent enzyme but also increased the maximal enzyme activity more than did direct addition of metal ions. Ferritin and metallothionein contributed to the activation of alkaline phosphatase with the metal ions. Since the binding of Zn2+ and Mg2+ to the nascent alkaline phosphatase is disturbed in Reuber rat hepatoma cells (R-Y121B), the apoenzyme is accumulated inside the cells. The binding of Zn2+ and Mg2+ to the apoenzyme readily takes place in the cell homogenates accompanied by an increase in catalytic activity without new enzyme synthesis.
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PMID:Activation of alkaline phosphatase with Mg2+ and Zn2+ in rat hepatoma cells. Accumulation of apoenzyme. 380 40

Ferritin binds a large quantity of Be2+ (Price D.J. and Joshi, J.G. J. Biol. Chem. 258 (1983) 10873) as well as other divalent metal ions. Therefore the ability of this protein to protect enzymes against or reverse the inhibition by metal ions was studied. Evidence presented here shows that the inhibition by Be2+ of the enzymes Na+K+ATPase, alkaline phosphatase and phosphoglucomutase is reversed by ferritin. Be2+ can be transferred reversibly between phosphoglucomutase and ferritin depending upon the relative concentrations of the 2 proteins. Ferritin also reactivated phosphoglucomutase inhibited by Zn2+, Cu2+, or Cd2+. Incubation of ferritin containing Be2+ with 4-10 fold molar excess of phosphoglucomutase (with respect to Be2+) removed 90% of the Be2+ from ferritin. The rates of inactivation of phosphoglucomutase by Be2+ donated by apoferritin or ferritin were identical. Based upon these observations it is suggested that Be2+ bound to the protein shell and to the iron core are in equilibrium with each other with the equilibrium favoring ferritin-Be2+ complex.
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PMID:Ferritin: protection of enzymatic activity against the inhibition by divalent metal ions in vitro. 633 Sep 34

The intestine of lambs killed immediately after birth and at intervals after the first feed was studied by electron microscope cytochemistry. Ferritin, incorporated into this feed, was found within 2 h of feeding within vesicles throughout the cytoplasm of enterocytes lining the proximal and mid-intestine. Some of these vesicles had fused with the lateral and basal membranes of the enterocytes. Histochemical reaction products for alkaline phosphatase and a series of lysosomal enzymes were localized within the vesicles; the distribution of acid hydrolases, however, was not uniform within each cell. Biochemical estimations of the activity of these enzymes showed greatest activity in the distal intestine of the newborn lamb. The activity of only one of these enzymes, N-acetyl-beta-glucosaminidase, was maximal in the mid-intestine. These observations indicate that cytoplasmic vesicles, translocating proteins across the enterocyte, probably carry intestinal alkaline phosphatase activity in their limiting membrane. Lysosomal enzymes, particularly glucosaminidase, are introduced into these vesicles as they traverse the enterocytes of the mid-intestine. A less specialized complement of lysosomal enzymes is probably introduced into vesicles in the distal intestine where ingested protein may be digested, rather than transported across the cell.
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PMID:Enzymes involved in protein transmission by the intestine of the newborn lamb. 712 59

In cultured rat hepatocytes the degradation of phosphoenolpyruvate carboxykinase mRNA might be regulated by protein(s), which by binding to the mRNA alter its stability. The 3'-untranslated region of phosphoenolpyruvate carboxykinase mRNA as a potential target was used to select RNA-binding protein(s) from rat liver by the use of gel retardation assays. A cytosolic protein was isolated, which bound to the phosphoenolpyruvate carboxykinase mRNA 3'-untranslated region and other in vitro synthesized RNAs. The protein was purified to homogeneity; it had an apparent molecular mass of 400 kDa and consisted of identical subunits with an apparent size of 24.5 kDa. Sequence analysis of a tryptic peptide from the 24.5-kDa protein revealed its identity with rat ferritin light chain. Binding of ferritin to RNA was abolished after phosphorylation with cAMP-dependent protein kinase and was augmented after dephosphorylation with alkaline phosphatase. Weak binding was observed in extracts from okadaic acid-treated cultured hepatocytes compared with untreated cells. Preincubation of ferritin with an anti-phosphoserine or an anti-phosphothreonine antibody attenuated binding to RNA, while an anti-phosphotyrosine antibody generated a supershift indicating that phosphoserine and phosphothreonine but not phosphotyrosine residues were in close proximity to the RNA-binding region. Ferritin is the iron storage protein in the liver. Binding of ferritin to RNA was diminished in the presence of increasing iron concentrations, whereas the iron chelator desferal was without effect. It is concluded that ferritin might function as RNA-binding protein and that it may have important functions in the general regulation of cellular RNA metabolism.
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PMID:Purification of a RNA-binding protein from rat liver. Identification as ferritin L chain and determination of the RNA/protein binding characteristics. 924

Ferritin and ferritin-binding proteins in canine serum were characterized. A certain percentage of ferritin in canine serum, but no tissue ferritin, was precipitated by centrifugation at 16,000 x g for 30 min. The precipitated ferritin was found to contain two subunits corresponding to the H and L subunits of canine liver ferritin by immunoblotting, the H subunit being predominant. More ferritin was precipitated from canine sera which had been incubated with anti-rat liver ferritin antibody than from untreated sera, and the H chain also predominated. To evaluate the possibility that the autoantibody was responsible for the precipitation of canine serum ferritin, the ferritin-binding activities of canine antibodies were examined using liver ferritin-coated microtiter plates and alkaline phosphatase-labeled antibodies specific for canine IgM, IgA, and IgG heavy chains. The results showed that IgM and IgA, but not IgG, had considerable ferritin-binding activities. Given these results, we suggest that there is H-chain-rich isoferritin in canine serum, and that ferritin exists as an immune complex.
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PMID:Characterization of ferritin and ferritin-binding proteins in canine serum. 1083 Dec 25

Ferritin-binding proteins (FBPs) in bovine serum were characterized by ferritin immunoassay, ferritin-binding activity, and immunoblotting. Serum ferritin, but not tissue ferritin, was precipitated by centrifugation at 14000 x g for 30 min, and bovine spleen ferritin added to bovine serum was precipitated by centrifugation at 1650 x g for 20 min. Two FBPs (FBP1 and FBP2) were purified from bovine serum by sequential chromatography on bovine spleen ferritin-Sepharose 4B affinity and Sephacryl S-300 columns. FBP1 separated into 82 kDa- and 26 kDa-bands on SDS-PAGE, while FBP2 separated into 55 kDa- and 26 kDa-bands. FBP1 and FBP2 were identified as IgM and IgG, respectively, by immunoblotting with alkaline phosphatase-labeled antibodies specific for bovine IgM, IgG, and IgA heavy chains. Given these results, we suggest that bovine FBPs are autoantibodies (IgM and IgG) to ferritin and that circulating ferritin exists as an immune complex.
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PMID:Characterization of bovine serum ferritin-binding proteins. 1512 10

Ferritin-binding protein (FBP) is known to interact with circulating ferritins in mammals. Canine FBPs were purified from canine serum by affinity chromatography and were identified as IgM, IgG, and IgA by immunoblotting with alkaline phosphatase-labeled antibodies to canine IgM, IgG, and IgA heavy chains. Following further purification by application to a Sephacryl S-300 column, canine FBPs were separated into 81.3- and 27.7-kDa bands by sodium dodecyl sulfate-polyacryamide gel electrophoresis, and the 81.3-kDa band reacted with the anti-canine IgM heavy chain antibody. Purified canine FBP bound to canine liver ferritin, but not to canine albumin and transferrin. FBP showed greater binding to the expressed bovine ferritin H-chain homopolymer than to the expressed bovine ferritin L-chain homopolymer. The binding of FBP with canine liver ferritin was dose-dependently inhibited by anti-rat liver ferritin antibody, and the anti-ferritin antibody dissociated the bound FBP in a dose-dependent manner, even after binding FBP with liver ferritin. The canine ferritin H subunit peptide fragment with amino acid residues 148-155 (NH(2)-GDHVTNLR-COOH) in its C-terminal region was recognized by FBP. These results indicate that canine serum FBPs are autoantibodies to ferritin (IgM, IgG, and IgA) and that anti-ferritin autoantibody (IgM) recognizes the C-terminal region of ferritin H subunit.
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PMID:Purification and characterization of canine serum ferritin-binding proteins. 1679 69


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