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)

Adenosine 2',5'-bisphosphate (pAp) is present in liver from 2-day-fasted rats, at a concentration of around 1 microM. pAp was obtained through perchloric acid extraction of the liver followed by two successive DEAE-cellulose chromatographies and an ion-pair high-pressure liquid chromatography. Both pAp extracted from liver and that obtained from a commercial source showed the same pattern of hydrolysis by alkaline phosphatase, i.e., more 5'-AMP than 2'-AMP was obtained as an intermediate of the reaction.
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PMID:Occurrence of adenosine 2',5'-bisphosphate in rat liver. 395 75

Alkaline phosphatase of matrix vesicles isolated from fetal bovine epiphyseal cartilage was purified to apparent homogeneity using monoclonal antibody affinity chromatography. The enzyme from the butanol extract of matrix vesicles bound specifically to the immobilized antibody-Sepharose in the presence of 2% Tween 20 whereas the major portion of nonspecific protein was removed by this single step. Of various agents tested, 0.6 M 2-amino-2-methyl-1-propanol, pH 10.2, was the most effective in eluting 80-100% of the enzyme initially applied. Both Tween 20 and 2-amino-2-methyl-1-propanol associated with the eluted enzyme were effectively removed by the sequential application of DEAE-cellulose and Sepharose CL-6B chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the enzyme preparation treated with sodium dodecyl sulfate and mercaptoethanol showed the presence of a dominant band (using silver staining) corresponding to a molecular weight of 81,000. This molecular weight was nearer reported values for rat liver (Ohkubo, A., Langerman, N., and Kaplan, M. M. (1974) J. Biol Chem. 249, 7174-7180) and porcine kidney (Cathala, G., Brunel, C., Chapplet-Tordo, D., and Lazdunski, M. (1975) J. Biol. Chem. 250, 6040-6045) alkaline phosphatase, than to previously reported values for chicken (Cyboron, G. W., and Wuthier, R. E. (1981) J. Biol. Chem. 256, 7262-7268) and fetal calf (Fortuna, R., Anderson, H. C., Carty, R. P., and Sajdera, S. W. (1980) Calcif. Tissue Int. 30, 217-225) cartilage matrix vesicle alkaline phosphatase. The purified alkaline phosphatase was activated by micromolar Mg2+. The amino acid composition of cartilage alkaline phosphatase was found to be similar to that previously described for porcine kidney (Wachsmuth, E. D., and Hiwada, K. (1974) Biochem. J. 141, 273-282). Double immunoprecipitation data indicated that monoclonal antibody against cartilage alkaline phosphatase cross-reacted with fetal bovine liver or kidney enzyme but failed to react with calf intestinal or rat cartilage enzyme. Thus these observations suggest that alkaline phosphatase of matrix vesicles from calcifying epiphyseal cartilage is a liver-kidney-bone isozyme.
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PMID:Purification and partial characterization of alkaline phosphatase of matrix vesicles from fetal bovine epiphyseal cartilage. Purification by monoclonal antibody affinity chromatography. 396 87

An enzyme that converts [3H, 32P]ATP, with a 3H:32P ratio of 1:1, to oligoadenylates with the same 3H:32P ratio was increased in plants following treatment with human leukocyte interferon or plant antiviral factor or inoculation with tobacco mosaic virus. The enzyme was extracted from tobacco leaves, callus tissue cultures, or cell suspension cultures. The enzyme, a putative plant oligoadenylate synthetase, was immobilized on poly(rI) . poly(rC)-agarose columns and converted ATP into plant oligoadenylates. These oligoadenylates were displaced from DEAE-cellulose columns with 350 mM KCl buffer, dialyzed, and further purified by high-performance liquid chromatography (HPLC) and DEAE-cellulose gradient chromatography. In all steps of purification, the ratio of 3H:32P in the oligoadenylates remained 1:1. The plant oligoadenylates isolated by displacement with 350 mM KCl had a molecular weight greater than 1000. The plant oligoadenylates had charges of 5- and 6-. HPLC resolved five peaks, three of which inhibited protein synthesis in reticulocyte and wheat germ systems. Partial structural elucidation of the plant oligoadenylates has been determined by enzymatic and chemical treatments. An adenylate with a 3',5'-phosphodiester and/or a pyrophosphoryl linkage with either 3'- or 5'-terminal phosphates is postulated on the basis of treatment of the oligoadenylates with T2 RNase, snake venom phosphodiesterase, and bacterial alkaline phosphatase and acid and alkaline hydrolyses. The plant oligoadenylates at 8 X 10(-7) M inhibit protein synthesis by 75% in lysates from rabbit reticulocytes and 45% in wheat germ cell-free systems.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Plant oligoadenylates: enzymatic synthesis, isolation, and biological activities. 399 78

A procedure for the purification of alkaline phosphatase from human polymorphonuclear leukocytes is described, involving enzyme solubilisation with Triton X-100 and chromatography on DEAE-Sepharose CL 6B and Cibacron Red F = B-Sepharose 4B. The final enzyme preparation was 244-fold purified and was shown to be capable of hydrolysis of a wide range of phosphorylated substates.
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PMID:Purification and properties of alkaline phosphatase from human polymorphonuclear leukocytes. 400 37

The main alkaline phosphatase isoenzymes of human bile have been purified by DEAE-cellulose chromatography. Characteristics of the isoenzymes, such as electrophoretic mobility before and after butanol extraction, Michaelis constant, and change in electrophoretic mobility following exposure to neuraminidase have been studied and compared with isoenzymes from other sources. The results show that the main alkaline phosphatase of bile is derived from the liver. It is present as a protein phosphatidylcholine complex.
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PMID:The nature of the alkaline phosphatases of bile. 411 11

1. Pneumococcal C-substance was isolated from the non-capsulated Pneumococcus 1-192R, A.T.C.C. 12213, by extraction with trichloroacetic acid solution followed by chromatography on DEAE-cellulose (HCO(3) (-) form). 2. The polymer contains 7.0% of phosphorus and 6.0% of nitrogen and is composed of phosphate, N-acetyl-d-galactosamine, d-glucose, N-acetyldiaminotrideoxyhexose, ribitol and choline in the molecular proportions 2:1:1:1:1:1. 3. After acid hydrolysis, d-galactosamine hydrochloride and galactosamine 6-phosphate were isolated in crystalline form and crystalline derivatives of d-glucose and anhydroribitol were obtained. A product of partial acid hydrolysis was provisionally characterized as 6'-O-phosphoryl-[O-beta-d-galactosaminyl-(1'-->6)-d-glucose]. 4. C-substance contains free amino groups accessible to attack by 1-fluoro-2,4-dinitrobenzene and nitrous acid. 5. Choline phosphate and ribitol phosphate are units in the polymer. 6. Treatment with hot alkali gave a fragment comprising phosphate, d-galactosamine, d-glucose, diaminotrideoxyhexose and ribitol in the molecular proportions 2:1:1:1:1. 7. After selective N-acetylation, the fragment contained one of its phosphate groups as a phosphomonoester and one as a phosphodiester, shown by potentiometric titration and by treatment with a phosphomonoesterase. 8. C-substance from seven other strains of Pneumococcus possesses a structure common to that described for the strain 1-192R. 9. Capsular materials from 26 different strains of Pneumococcus were analysed for suspected contamination by C-substance. In 19 cases the presence of C-substance with the normal structure was demonstrated, and in the remaining seven cases the contaminating C-substance was probably similarly constituted. 10. F-substance was isolated and the associated fatty acid material analysed.
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PMID:Pneumococcal C-substance, a ribitol teichoic acid containing choline phosphate. 438 89

Alkaline phosphatase (EC 3.1.3.1) from pig kidney brush-border membranes was solubilized from membrane precipitates by butan-1-ol at a critical pH of 7.0. The 12000-fold purification procedure included (NH(4))(2)SO(4) precipitation, DEAE-and TEAE-cellulose chromatography, Sephadex G-200 gel filtration and neuraminidase digestion followed by DEAE-cellulose chromatography. The purified protein contained 20% (w/w) carbohydrate and had mol.wt. 150000-156000 as estimated by Sephadex filtration and ultracentrifuge analysis. It was a tetrameric glycoprotein consisting of identical subunits, and it had a molecular activity at 25 degrees C of 2600s(-1) per tetramer. Its concentration in kidney was estimated to be 8.5-8.8mg/kg.
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PMID:Alkaline phosphatase from pig kidney. Method of purification and molecular properties. 445 5

Several alkaline phosphatases (EC 3.1.3.1) could be obtained from pig kidney brush-border membrane on extraction with butan-1-ol. Three of the multiple forms were separated by DEAE-cellulose chromatography and further purified. They form a regular series with different degrees of glycosylation (mainly owing to N-acetylneuraminic acid), of charge, of molecular weight, of stability to temperature, to pH and to urea, of minimal requirement for Mg(2+) and of extractability by butan-1-ol. In contrast, the detectable antigenic sites, the inhibition by amino acids and the pH-dependency of K(m) and V(max.) were identical for these multiple forms. On treatment with neuraminidase, the multiple forms became identical in all their properties. It was therefore concluded that the microheterogeneity of alkaline phosphatase is due to different degrees of glycosylation at polypeptide chains which appear to be otherwise identical.
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PMID:Alkaline phosphatase from pig kidney. Microheterogeneity and the role of neuraminic acid. 445 6

To characterize the biological changes which result in increased granulocyte alkaline p-nitrophenyl phosphatase activity in patients with polycythemia vera, the enzyme was purified from granule fractions of sucrose homogenates made from dextran-sedimented leukocytes of normal subjects and patients with polycythemia vera. Polycythemic blood yielded 3-10 times as much granulocyte alkaline phosphatase per 10(9) leukocytes as did normal blood. Sodium dodecyl sulfate extracts of granules were purified by DEAE-cellulose chromatography and sucrose gradient centrifugation to apparent homogeneity as judged by polycarylamide disk gel electrophoresis. Granulocyte alkaline phosphatase from normal subjects was purified 6910-fold with a 60% yield and a specific activity of 47 U/mg. Granulocyte alkaline phosphatase from polycythemic patients was purified 1.166-fold with a 50% yield and a specific activity of 70 U/mg. The two enzymes did not differ in molecular weight; both appeared to be about 160,000 daltons by sucrose gradient centrifugation. Both appeared to be zinc metalloenzymes, in that they were specifically inhibited by o-phenanthroline. Their elution requirements when adsorbed to DEAE-cellulose suggested they were lipoproteins although the content of phosphorus was below the threshold of detection. The identity of the two enzymes was suggested by immunological studies in which antibody prepared against purified polycythemia vera enzyme gave a precipitation reaction of identity with another polycythemia vera enzyme and two pools of normal enzyme. It is possible to account for the difference in alkaline phosphatase activity between the granulocytes of patients with polycythemia vera and normal subjects by differences in the quantity of enzyme synthesized.
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PMID:Granulocyte alkaline phosphatase. Studies of purified enzymes from normal subjects and patients with polycythemia vera. 473 97

A pancreatic ribonuclease digest of (14)C-labeled tobacco necrosis virus RNA was fractionated according to charge by column chromatography. Individual fractions were dephosphorylated with alkaline phosphatase and rechromatographed. The fraction, originally containing oligonucleotides with seven negative charges, separated into two components corresponding to five (-5) and two negative charges (-2). The -5 fraction was derived from the internal oligonucleotides while the -2 fraction must have originated from a 5'-pyrophosphorylated terminal trinucleotide. The sequence of this terminal trinucleotide was determined by column chromatography on DEAE-cellulose in a triethyl ammonium carbonate gradient, using the appropriate markers. The radioactivity chromatographed with a (ApGp)U marker. The order of the Ap and Gp was determined after ribonuclease T(1) and alkaline phosphatase digestion. The radioactivity in the product chromatographed with an ApG marker. The 5'-terminus of tobacco necrosis virus RNA was therefore determined as ppApGpUp..., which is identical to the terminus of the RNA of its satellite virus as previously determined (J. Mol. Biol., 38, 59 (1968); Science, 160, 1452 (1968)). The 5' pyrophosphate in both viruses was probably formed by an in vivo enzymatic removal of a gamma-phosphate from a triphosphate, and its presence in both viruses suggested a common site of synthesis. The identity of the 5'-terminal sequences is considered not to be fortuitous and is discussed from the standpoint of their role as a recognition site for the virus-specific RNA replicase.
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PMID:Identity of the 5'-terminal RNA nucleotide sequence of the satellite tobacco necrosis virus and its helper virus: possible role of the 5'-terminus in the recognition by virus-specific RNA replicase. 527 92


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