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:3.1.25.1 (deoxyribonuclease)
1,471 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Purpura was grossly observable in albino mice 6 to 8 h after the intraperitoneal injection of sterile, deoxyribonuclease-treated, cell-free extracts prepared by sodium deoxycholate-induced lysis, sonic disruption, Parr bomb treatment, autolysis without sodium deoxycholate, or alternate freezing and thawing of washed suspensions of Streptococcus pneumoniae type I. Cell-free extracts obtained from sonically disrupted, heat-killed cells (100 degrees C for 20 min) did not contain purpurogenic activity. The reaction was maximal at approximately 24 h postinjection, started to fade slowly after 24 to 48 h, and usually was not grossly observable by 4 to 6 days postinjection. The purpura-producing principle (PPP) in the cell-free extract was purified by sequential ammonium sulfate precipitation, protamine sulfate precipitation, Sepharose 6B gel filtration, wheat germ lectin-Sepharose 6MB affinity chromatography, ribonuclease and trypsin treatment, and a second Sepharose 6B gel filtration step. The final preparation (i) contained glucosamine (5.6%), muramic acid (8.0%), neutral carbohydrate (12.8%), phosphate (8.0%), orcinol-reactive material (6.0%), and Lowry-reactive material (1.6%), and (ii) was free of detectable amounts of deoxyribonucleic acid, capsular polysaccharide, neuraminidase, cytolysin, and hyaluronidase. The isoelectric point and molecular size of the PPP were approximately pI 3.0 and several million daltons, respectively, and the activity remained in the supernatant fluid after centrifugation for 1 day at 105,000 x g. PPP activity was destroyed by incubation with egg white lysozyme and sodium metaperiodate but was resistant to trypsin, pronase, alpha-amylase, deoxyribonuclease, ribonuclease, alkaline phosphatase, pancreatic lipase, 7% trichloroacetic acid, 6 M urea, autoclaving (121 degrees C) for 30 min, and mild acid and alkali exposure. Our observations indicate that the PPP requires intact beta-1,4-glucosidic linkages for activity and support the working hypothesis that activity is associated with pneumococcal peptidoglycan solubilized by the bacterium's autolysin.
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PMID:Characterization of pneumococcal purpura-producing principle. 624 53

All strains of Legionella pneumophila tested produced detectable levels of extracellular protease, phosphatase, lipase, deoxyribonuclease, ribonuclease, and beta-lactamase activity. Weak starch hydrolysis was also demonstrated for all strains. Elastase, collagenase, phospholipase C, hyaluronidase, chondroitinase, neuraminidase, or coagulase were not detected in any of these laboratory-maintained strains.
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PMID:Extracellular enzymes of Legionella pneumophila. 626 49

The effect of various treatments on the activity of anti-treponemal lymphotoxin (ATL) produced by lymphocytes of syphilitic rabbits was studied. Treponema pallidum-killing activity of ATL was slightly reduced after heating at 56 degrees C and completely abolished at 100 degrees C. The significant reduction of the activity was also obtained after exposure of ATL to acidic conditions (pH 1-5) at room temperature, or by treatment with papain and neuraminidase. Activity of ATL was completely resistant to deoxyribonuclease, ribonuclease and trypsin treatment. ATL was eluted from the Sephadex G-100 column together with hemoglobin, that suggested the apparent molecular weight of ATL of about 65,000. The active fraction from the Sephadex G-100 column was further fractionated on DEAE-Sephadex A-50. The activity of ATL was widely spread in the column eluate, indicating the charge heterogeneity. All these data indicate that ATL is a relatively low molecular weight protein. The sensitivity to neuraminidase and heterogeneity of charge suggest that it is a glycosylated protein.
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PMID:Characterization of anti-treponemal lymphotoxin from lymphocytes of syphilitic rabbits. 638 57

The noncytotoxic immunosuppressive substance detected in crude extracellular products of Streptococcus intermedius (CEP-SI) was fractionated by two steps of preparative isoelectric focusing in sucrose gradients using ampholytes of pH range from 3.5 to 6 and 4 to 5, respectively. The in vitro and in vivo suppressor effects of the most highly purified fraction of CEP-Si, designated fraction 3' (F3'EP-Si), corresponded well with those of the original CEP-Si. F3'EP-Si was sensitive to the effects of alpha, gamma, and delta chymotrypsin, trypsin, and heating. It contained approximately 1% of the total amount of protein found in the original CEP-Si, corresponding to a single band on analytical isoelectric focusing, stainable by Coomassie Blue and of isoelectric point of 4.25. The absorption spectrum of F3'EP-Si had a maximum at 260 nm but its biological activity was resistant to deoxyribonuclease and ribonuclease A and it did not contain material stainable by methylene blue. It was also resistant to neuraminidase and did not contain material stainable by periodic acid schiff. We conclude that the substance responsible for the suppressor activity of CEP-Si is a protein of molecular weight approximately 90,000, which adheres to Sephadex of cellulose acetate and forms complexes with other, nonactive constituents of CEP-Si.
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PMID:Fractionation and characterization of the immunosuppressive substance in crude extracellular products released by Streptococcus intermedius. 645 98

The binding of human 125I-labeled lactoferrin (LF) to a population of adherent mononuclear cells (ADMC) and nonrosetting lymphocytes (E-) was abolished by prior treatment of the cells with deoxyribonuclease (DNase), but not ribonuclease (RNase). When DNase-treated ADMC were incubated with exogenous DNA, the binding of 125I-LF was restored. Enzymatic digestion with other enzymes, trypsin, phospholipase D, and neuraminidase, did not significantly influence 125I-LF binding. Saturable binding of LF at 0 degrees C was demonstrated for both E- and ADMC, with equilibrium dissociated constants of 0.76 x 10(-6) M and 1.8 x 10(-6) M, respectively. E- cells bound 2.5 x 10(7) and ADMC bound 3.3 x 10(7) molecules of Lf at saturation. Cell membranes were isolated from ADMC, E- and E+ and reacted with 125I-labeled LF; significant binding was only seen with ADMC and E-. Prior treatment of the membranes with DNase abolished the binding. Immunofluorescence studies indicated that a population of ADMC and E-, but not E+, exhibited a peripheral staining pattern for LF. Prior treatment of ADMC and E- with DNase abolished the surface immunofluorescence. This study provides evidence that cell membrane DNA acts as a binding site for exogenous LF. This is a novel role for DNA that has not been previously reported. Furthermore, it points to a basic difference between E+ cells vs. ADMC and E- cells in respect to their possession of cell surface DNA.
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PMID:Lactoferrin binds to cell membrane DNA. Association of surface DNA with an enriched population of B cells and monocytes. 660 Jul 47

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

Homogenates of human pancreas in saline were centrifuged at 27 000 X g and the supernates were fractionated by preparative polyacrylamide gel electrophoresis. The gels were divided into sections and each section was injected into rabbits; after absorption with polymerized serum from apparently normal humans, the antiserum obtained by injecting one of the sections was tested against a variety of human tissue extracts but reacted only with saline extracts of human pancreas. The absorbed antiserum, polymerized and made insoluble with glutaraldehyde, was used to purify a pancreas-specific antigen by immunoaffinity batch technique. The purified antigen proved to be a protein with some carbohydrate content (180 mg/g by weight) and a molecular mass of about 2.25 X 10(5) daltons. The antigen is relatively thermostable, and precipitates in the range of 245.64-340.2 g/L saturated ammonium sulfate; its antigenic activity is not affected by incubation with ribonuclease or deoxyribonuclease, but is destroyed by incubation with trypsin or neuraminidase and by extraction with perchloric acid. Immunofluorescence studies show that the antigen is diffusely present in the cytoplasm of pancreatic acinar cells.
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PMID:Isolation and characterization of a human pancreas-specific protein. 698 12

By using a suckling mouse assay, heat-stable enterotoxin (ST) was purified from the culture filtrate of Yersinia enterocolitica isolated from a diarrheal patient. The purification procedures involve ultrafiltration with an Amicon HIP-10 hollow fiber, ethanol fractionation, protamine sulfate treatment, diethylaminoethyl-Sephacel and hydroxylapatite column chromatographies, and Sephacryl S-200 superfine gel filtration. About 408-fold purification was achieved, with a yield of 12.0%. The minimal effective dose of purified ST was about 110 ng in the suckling mouse assay. The molecular weight of purified ST was 9,000 by Sephadex G-100 superfine gel filtration. The purified ST was stable to heating (100 degrees C for 20 min, 121 degrees C for 20 min) and did not lose its toxicity after treatment with protease, trypsin, lipase, phospholipase C, ribonuclease, deoxyribonuclease, beta-glucosidase, and neuraminidase. The purified ST was separated by isoelectric focusing into two active fractions, with pI's of 3.29 (ST-1) and 3.00 (ST-2), respectively. Antiserum from guinea pigs immunized with the purified ST neutralized the activity of both Y. enterocolitica ST and Escherichia coli ST.
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PMID:Partial purification and characterization of heat-stable enterotoxin produced by Yersinia enterocolitica. 721 60

This paper describes the analysis of recombinant human deoxyribonuclease (rhDNAse), an acidic and complex phosphoglycoprotein, by capillary zone electrophoresis (CZE). Separation performance was found to be dramatically improved by the addition of calcium ions to the CZE running buffer, due to the influence of calcium binding on the charge and the electrophoretic behavior of rhDNAse. The pH dependent calcium binding effects on the electrophoretic separation were demonstrated at both acidic and basic pH, resulting in a two-dimensional (pH 4.8 and 8.0) calcium aided analysis that achieved multipeak resolution of the complex, glycosylation based, charge microheterogeneity of rhDNAse. Two-dimensional investigation of neuraminidase- and alkaline phosphatase-digested protein further demonstrated that the acidic pH resolved acidic charge heterogeneity and that the basic pH discriminated neutral heterogeneity. This work demonstrates the resolving power of CZE for the analysis of a complex microheterogeneous glycoprotein, and emphasizes the importance of employing multiple separation conditions in accordance with known structural characteristics of the protein.
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PMID:Use of acidic and basic pH and calcium ion addition in the capillary zone electrophoretic characterization of recombinant human deoxyribonuclease, a complex phosphoglycoprotein. 1048 37

From saline extracts of Phytolacca esculenta (shoriku) roots, two phytomitogenes were isolated by salting out with (NH4),SO4 and chromatography on DEAE-cellulose and Sephadex G-100 columns. Both fractions were homogeneous on disc electrophoresis and on immunoelectrophoresis. One of these (Fraction E-2) was shown to be similar to pokeweed mitogen in respect to mol. wt (32,000) and amino acid composition. The other (Fraction E-3) was a protein of 18,000 mol. wt. Both fractions had similar biological activities to pokeweed mitogen in their ability to stimulate pig blood lymphocytes in vitro to incorporate tritiated thymidine, and to induce blastoid transformation. Both fractions contained an unusually large amount of cystine, i.e., 18 half-cystine residues % for Fraction E-2 and 22 residues % for Fraction E-3. Although these mitogens were resistant to deproteinizing procedures such as perchloric acid treatment and Sevag's procedure, the DNA synthesis-stimulating activity was inactivated by digestion with Pronase E and Nagarse, but resistant to trypsin, chymotrypsin, deoxyribonuclease, ribonuclease, lysozyme and neuraminidase. The activity was stable at acidic and neutral pH (4-7) but unstable at alkaline pH. The activity at pH 7.3 was stabilized by the addition of Ca2+ or Mg2+. On the addition of more than 2 mM of Ca2+, precipitation of mitogen occurred. From the above results the molecular basis of the mitogenic activity of shoriku mitogen is discussed.
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PMID:Isolation and characterization of pokeweed mitogen-like phytomitogens from Shoriku, Phytolacca esculenta. 1999 19


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