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)

Column chromatographic purification and sensitivity towards enzymatic treatments of dialyzable transfer factor (TFd), the immunologically specific component of dialyzable leukocyte extract (DLE), have previously been used in its biochemical characterisation. In the present work we studied the effect of enzymes and the Sephadex G-10 chromatographic separation of the components of DLE augmenting delayed-type hypersensitivity. Skin reactivities to streptokinase-streptodornase (SK-SD) and tuberculin PPD were significantly augmented by injecting DLE into antigen-primed guinea pigs. The augmentation caused by DLE treatment correlated to the pre-existing level of immunity in the recipients. Most of the augmentory activity resided in 2 adjacent fractions, eluting early from a Sephadex G-10 column. This augmentation was destroyed by alkaline hydrolysis, by treatment with pronase, proteinase K, ribonuclease, and nuclease P1, but not by alkaline phosphatase or phosphodiesterase II. The observed sensitivities towards these enzymes, except that for ribonuclease, were closely similar to those described for the specific TFd component of DLE. These results are compatible with the idea that either the nonspecific augmenting and the specific TFd molecules are principally similar, or that the TFd molecules, in addition to their capacity to transfer specific immunity, also have an augmenting effect, which needs in its manifestation a sub-threshold dose of immunogen.
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PMID:Augmentation of delayed-type hypersensitivity in antigen-primed guinea pigs by human dialyzable leukocyte extract. Chromatographic and enzymatic characterization of the active principle. 676 49

The pep4-3 mutation results in a 90-95% reduction in the levels of five vacuolar hydrolases in yeast, including proteinases A and B, carboxypeptidase Y, RNase(s) and the repressible alkaline phosphatase. The mutation is without effect on two secreted glycoproteins, on an enzyme of the vacuolar membrane, and on a proteinase located outside of the vacuole. Mutations at the PEP4 locus exhibit a dosage effect on the levels of some, but not all, of the enzymes whose expression requires the function of the gene.
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PMID:PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae. 676 1

A pancreas-specific antigen was identified by immunologic techniques and purified from saline extract of human pancreas. The purified pancreas-specific antigen was shown to be homogeneous by polyacrylamide gel electrophoresis under both denaturing and non-denaturing conditions. It had a molecular weight of 44000 as estimated by gel filtration or sodium dodecyl sulfate-gel electrophoresis, and a sedimentation coefficient of 3.4 S as analyzed by sucrose gradient centrifugation. Pancreas-specific antigen possessed an isoelectric point of 4.9 and migrated to alpha-beta region upon immunoelectrophoresis. By colorimetric assay procedures, pancreas-specific antigen exhibited no enzyme activity, such as amylase, protease, esterase, lipase, acid phosphatase, alkaline phosphatase peroxidase, deoxyribonuclease or ribonuclease. Immunoreactivity of pancreas-specific antigen was sensitive to proteolytic enzymes, perchloric acid and high temperature (70 degrees C, 10 min); but insensitive to neuraminidase or beta-glucosidase. Immunohistochemical staining revealed that pancreas-specific antigen was located in acinar cells of human pancreas. In addition, a higher concentration of pancreas-specific antigen was detected in pancreatic juice than in the saline extract of pancreas. This newly identified pancreas-specific antigen, therefore, may be a useful marker protein in physiological studies of pancreas and pancreatic secretion.
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PMID:Purification and characterization of a human pancreas-specific antigen. 678 69

Low dosages of chloramphenicol (25-50 micrograms/ml) brought about a 2-4-fold stimulation of acid phosphatase activity in 48 h-germinated cotton (Gossypium hirsutum) embryos. However, at high concentrations of chloramphenicol (100-1000 micrograms/ml), there was a progressive decline in enzyme activity. The stimulatory effect of the drug on acid phosphatase activity was relatively specific, since no significant stimulation of activities of proteinase, deoxyribonuclease, ribonuclease, o-diphenolase and peroxidase was observed in germinating cotton embryos. Chloramphenicol, however, did promote the activities of isocitric lyase and alkaline phosphatase. Sephadex G-200 chromatography of the enzyme fraction revealed high (230 000)- and low (106 000)-molecular-weight multiple forms of acid phosphatase in the chloramphenicol-treated embryos, in contrast with a single molecular form (mol.wt. 106 000) in the untreated embryos. Thus the treatment of cotton embryos with chloramphenicol induced both a qualitative and a quantitative change in the acid phosphatase activity. Chloramphenicol-stimulated acid phosphatase activity was strongly inhibited when Pi was included in the germination medium. However, the control embryos showed less pronounced inhibition of enzyme activity in presence of Pi ions.
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PMID:Chloramphenicol stimulates acid phosphatase activity in germinating cotton (Gossypium hirsutum) embryos. 687 Aug 57

Mouse L-cell nuclei incorporate gamma-32P from ATP in vitro predominantly in 5'-monophosphoryl termini and internal phosphodiester bonds with a nonrandom nearest-neighbor distribution. In the presence of 1 microgram of alpha-amanitin per ml the gamma-32P showed a time-dependent appearance in RNA bands which migrated with mature tRNA species but not with pre-tRNA and 5S RNA. The gamma-32P was found in internal phosphodiester bonds as shown by alkaline phosphatase resistance and was identified in 3'-monophosphates after RNase T2, T1, and A digestion. The specificity of this incorporation was indicated by a limited number of labeled oligonucleotides from a T1 digest and identification of 70 to 80% of the 32P label as Cp on complete digestion of the eluted tRNA band. We also observed transiently [gamma-32P]ATP-labeled RNA bands (in 5'-monophosphate positions) that were 32 to 45 nucleotides long. The results presented suggest splicing of several mouse L-cell tRNA species in isolated nuclei which involve the RNA 5'-OH kinase products as intermediates.
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PMID:Nuclear ligation of RNA 5'-OH kinase products in tRNA. 711 Jan 32

The effects of the sublethal concentration (0.012%) of Congo Red on Heteropneustes fossilis were studied after 30 days exposure. The RBC count haemoglobin (Hb)% and PCV decreased significantly. The total WBC count, MCV, MCH, and MCHC showed a significant increase. Serum calcium, serum cholesterol and blood urea nitrogen (BUN) were significantly elevated, whereas serum phosphorus was significantly reduced. The activities of serum alkaline phosphatase (AlPase), acid phosphatase (AcPase). RNase, GOT, GPT and amylase were also significantly elevated. The possible reasons for these changes are discussed.
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PMID:Haematological and biochemical characteristics of Heteropneustes fossilis under the stress of Congo Red (diphenyl disazo binaphthionic acid). 716 84

In this paper clinical similarities between sickle cell anemia patients and zinc deficient subjects, the latter as reported from the Middle East have been presented. Zinc levels in plasma, red cells, hair and neutrophils were decreased in our adult patients with SCA. The activities of certain zinc dependent enzymes such as plasma RNase, red cell carbonic anhydrase, leucocyte alkaline phosphatase, and deoxythymidine kinase activity in freshly synthesized collagen connective tissue were consistent with the concept that indeed zinc deficiency occurred in SCA patients. Zinc supplementation under controlled conditions showed that the SCA patients gained weight, their serum testosterone level increased and plasma ammonia level decreased. Finally, we also observed abnormal dark adaptation in some SCA patients which improved following zinc supplementation. Inasmuch as we have previously reported that the number of irreversible sickle cells decrease following zinc supplementation, we would like to suggest that zinc supplementation at earlier age may be benefical in preventing organ damage. In conclusion, zinc supplementation should be prescribed for patients with SCA, particularly if they show evidences for zinc deficiency.
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PMID:Zinc deficiency and effects of zinc supplementation on sickle cell anemia subjects. 729 Dec 6

The effect of a low protein (4%) diet on the activity of the hydrolytic enzymes ribonuclease, deoxyribonuclease, acid and alkaline phosphatases, beta-glucuronidase and lysozyme has been studied in the spleen and thymus of weanling Wistar rats. Experimentation was carried out over 20 and 30 days, and comparisons were made with well-nourished (12% protein) controls. Body weight decreased during the terminal period in protein-deficient animals (P less than 0.001). Spleen and thymus absolute net weights also dropped significantly (P less than 0.001). In terms of organ weight relative to body weight, there was a clear decrease in thymus compared with controls (P less than 0.001). Enzyme activities expressed per total organ fell significantly. Thus, in spleen at 20 days the decrease was maximum in ribonuclease activity (91.15%) and minimum in acid phosphatase activity (44.09%). Thymus decreases ranged from 83.60% activity in beta-glucuronidase and 93.56% in ribonuclease. At 30 days decreases were accentuated; the maximum value in spleen was 92.34% lysozyme and, in thymus, 97.09% acid phosphatase. A large increase in hydrolytic activity expressed per milligram of protein was registered, especially at 30 days. This increase reached a maximum of 78.08% beta-glucuronidase in thymus and a minimum of 56.1% alkaline phosphatase; acid phosphatase and ribonuclease activities were not modified. In spleen, however, acid phosphatase (34.00%), alkaline phosphatase (62.50%), deoxyribonuclease (39.25%), and beta-glucuronidase (36.01%) increased, but lysozyme and ribonuclease enzymes decreased. We concluded that a low protein diet increases catabolism in spleen and thymus through an enhancement of lysosomal hydrolase activities.
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PMID:Effect of protein deficiency on the lysosomal enzyme activities of the spleen and thymus of weanling rats. 731 May 38

DNases A1 and A2 have been purified to homogeneity from the hepatopancreas of Achatina fulica by a series of steps: acetate buffer extraction, ammonium sulfate precipitation and column chromatography on hydroxylapatite, phosphocellulose, Blue-Sepharose, and poly(A)-Sepharose. The purified enzymes are free of acidic phosphomonoesterase, phosphodiesterase, and RNase activities. They are slightly acidic glycoproteins with identical isoelectric point (6.90). On 0.1% SDS gel electrophoresis, DNase A2 had a molecular weight of 30,000 when dissolved in 1% SDS, but it had molecular weights of 17,500, 8,000, and 4,800 when dissolved in 1% SDS and 1% 2-mercaptoethanol. This was evidence that the enzyme consists of three different subunits joined by interchain disulfide bonds. DNases A1 and A2 are endonucleases working at acidic pH (3.5--6.0) and do not require divalent cations for their activities. The enzymes degrade poly(dA) 5 times faster and poly(dT) 3 times faster than heat-denatured DNA under optimal conditions but do not appreciably digest poly(dG) and poly(dC). We developed an analytical procedure for oligodeoxynucleotides by high-performance liquid chromatography. The phosphomonoester end group and the mode of degradation were examined by the method. The termini produced by the enzymes have 3'-phosphoryl and 5'-hydroxy end groups. The products of exhaustive hydrolysis contain di-, tri-, tetra-, and pentanucleotides and mononucleotide was barely detected. The hydrolyzing activities of DNases A1 and A2 are stimulated by polyamines such as spermine, spermidine, and putrescine, but are inhibited by synthetic polynucleotides and various drugs. Adenosine deaminase highly active on oligoadenylic acids was found in a crude DNase A fraction. The enzyme preparation has higher activity on 3'-adenylic acid than on 5'-adenylic acid. The first adenosine residue of oligoadenylic acids was deaminated considerably more rapidly than the second or succeeding ones.
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PMID:DNase A, a poly(dA) and poly(dT)-specific deoxyribonuclease from Achatina fulica. Purification and characterization. 733 15

Plasma membrane from the brush border isolated from the tegument of Hymenolepis diminuta contains membrane-bound ribonuclease (RNase) and alkaline phosphatase activities. RNase (yeast RNA substrate), alkaline phosphatase (p-nitrophenyl phosphate substrate), and additional membrane proteins were solubilized by sonication or treatment with the detergents dodecyl trimethylammonium bromide, beta-octyl-D-glucopyranoside, sodium dodecyl sulfate (SDS), or ZwittergentTM 3-12 (N-dodecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate). At optimal conditions, greater than 90% of both enzymes and total protein were solubilized by the latter two detergents, whereas beta-octyl-D-glucopyranoside, dodecyl trimethylammonium bromide, and sonication were only partially effective. Nonionic detergents did not solubilize the membrane effectively.
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PMID:Solubilization of membrane-bound ribonuclease (RNAse) and alkaline phosphatase from the isolated brush border of Hymenolepis diminuta (Cestoda). 739 87


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