Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.21.1 (DNase)
7,655 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

231 Methicillin-Resistant Staphylococcus (MRS) and 76 Methicillin-Susceptible Staphylococcus (MSS) strains were investigated for Staphylococcal Protein A, bacteriocin, DNase and beta lactamase production properties. It was found that 73.6% of the strains of MRS were positive for protein A, 3.8% for bacteriocin, 76.2% for DNase and 84.4% for beta lactamase production. And it was found that 61.8% of MSS strains were positive for protein A, 11.8% for bacteriocin, 55.2% for DNase and 57.9% for beta lactamase production. Staphylococcal protein A, DNase and lactamase production. Staphylococcal protein A, DNase and lactamase production were found to be significantly higher in MRS strains than MSS strains and bacteriocin production was found to be higher in MSS strains than MRS strains according to Chi Square Test.
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PMID:[Staphylococcal protein A, bacteriocin, DNase and lactamases of methicillin-resistant Staphylococcus]. 174 46

The article deals with rapid agglutination tests for Staphylococcus aureus identification which detect clumping factor and protein A. The tests were compared with standard diagnostic methods: free coagulase, bound coagulase and thermostable deoxyribonuclease, 190 Staphylococcus aureus strains have been examined of which, 105 methicillin susceptible strains, 85 methicillin resistant strains, and 32 coagulase negative staphylococci strains strains. The presence of clumping factor was detected in 100% of examined Staphylococcus aureus strains. No difference between methicillin susceptible strains and methicillin resistant strains was observed. Protein A was present in 96.1% of methicillin susceptible strains and in 90.6% of methicillin resistant Staphylococcus aureus strains. The same test showed false negative results in 12 strains: 4 of which methicillin susceptible and 8 methicillin resistant strains. Coagulase test slide method and protein A detecting test hand one false positive result each for coagulase negative staphylococci examined. The specificity of all tests used was 100% and 99.5% respectively. The authors suggest latex or hemagglutination tests detecting clumping factor and/or protein A for rapid Staphylococcus aureus strains identification in hospital environment. It is important to point out the possibility of getting false negative protein A detecting results in methicillin resistant strains.
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PMID:[Rapid agglutination tests for the identification of Staphylococcus aureus]. 259 64

Catalytic antibodies (abzymes) which hydrolyze RNA and DNA were isolated from bovine colostrum by sequential chromatography on Protein A Sepharose, denaturated DNA-cellulose, Mono Q, and gel permeation chromatography on Superose 12 at pH 2.3 after acidic shock. Metachromatic agar containing toluidine blue and yeast RNA was used to measure RNase activity. Electrophoresis in agarose showed DNase activity on plasmid DNA from Escherichia coli and DNA from calf thymus in fractions from all 4 purification steps. Gel permeation chromatography showed that the abzymes hydrolysed both a single-stranded polyadenylic acid (Poly A) and single-stranded polycitidylic acid (Poly C), while partially purified RNase from the colostrum hydrolysed Poly (C), but not Poly (A). Electrophoresis of purified abzymes under denaturing conditions showed protein bands of molecular mass corresponding to heavy and light chains of IgG. The abzymes immunoreacted with anti-bovine IgG. The RNase activity of the purified abzymes represented 0.022% of total RNase activity in the colostrum; acid shock and gel filtration at low pH reduced the specific RNase activity of abzymes 3.6-fold. The RNase activity of abzymes at pH 6.6 was reduced by 90% by heat treatment at 75 degrees C for 52 min.
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PMID:Isolation and partial characterization of catalytic antibodies with oligonuclease activity from bovine colostrum. 1193 74

Linezolid is a new oxazolidinone with potent antibacterial activity against Gram-positive cocci; it uniquely inhibits bacterial translation through inhibition of 70S initiation complex formation. The effects of sub-growth-inhibitory concentrations of linezolid on the expression of various structural and soluble virulence factors of Staphylococcus aureus and Streptococcus pyogenes were examined. For S. aureus, strains Wood 46 and Cowan 1 (NCTC 8532) were used to measure protein A, coagulase, alpha-haemolysin (hla) and delta-haemolysin (hld). For S. pyogenes, strain NCTC 9994 was used to measure M protein, streptolysin O (SLO) and DNase. Coagulase was assayed by clotting of citrated rabbit plasma, and hla, hld and SLO by lysis of rabbit, human and horse erythrocytes, respectively. Protein A and M protein were measured indirectly using bacterial susceptibility to phagocytic ingestion of radiolabelled bacteria by human neutrophils. When S. aureus was grown in 1/2, 1/4 and 1/8 MIC, linezolid, coagulase, hla and hld production were impaired. Susceptibility to phagocytosis was changed by growth in the presence of 1/2 MIC linezolid compared with that in its absence (50.8 +/- 4.1% versus 38.9 +/- 2.9%; P <or= 0.05). When S. pyogenes was grown in 1/2, 1/4 and 1/8 MIC linezolid, SLO and DNase production were impaired compared with that of bacteria grown in the absence of the drug; its susceptibility to phagocytosis was also increased (52.8% bacteria ingested versus 37.5%; P <or= 0.05). A reduction in virulence factor expression at sub-MIC linezolid concentrations may be of benefit in the treatment of Gram-positive infections.
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PMID:Virulence factor expression by Gram-positive cocci exposed to subinhibitory concentrations of linezolid. 1240 22

Nucleoli were isolated from physarum polycephalum, and nucleolar matrix was prepared by digesting the nucleoli respectively with DNase 1, 0.25 mol/L (NH4)2SO4 and 2 mol/L NaCl to remove DNA and most proteins. SDS-PAGE analysis indicated that there were about 20 polypeptides in nucleolar matrix component, including the 37 kD polypeptide which was similar to tropomyosin in molecular weight. The result of indirect immunofluorescence treated with anti-tropomyosin antibody and sheep anti-rabbit IgG antibody labelled with FITC showed that bright fluorescence was observed in the nucleoli and nucleolar matrix, but no bright fluorescence in the controls. Indirect Immunoblotting detection further verified that tropomyosin existed in nucleolar matrix. Protein A-colloidal gold immunoelectron microscopic study showed that there were many gold particles in the specimens labelled with tropomyosin antibody, and there were few gold particles found in the controls. Tropomyosin distributed dispersedly in nucleoli.
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PMID:[Immunocytochemical identification of tropomyosin in nucleoli and nucleolar matrix of Physarum polycephalum]. 1255 20

Immunization of rabbits with DNase I leads to the production of antiidiotypic Abs with DNase activity. It is not known at present whether antiidiotypic Abs against DNA-hydrolyzing enzymes can possess RNase activity. Here we show that immunization of healthy rabbits with bovine DNase I produces IgGs with intrinsic DNase and RNase activities. Electrophoretically and immunologically homogeneous polyclonal IgGs were obtained by sequential chromatography of the immune sera on Protein A-Sepharose and gel filtration. Affinity chromatography on DNA cellulose using elution of Abs with different concentrations of NaCl and an acidic buffer separated catalytic IgGs into four Ab subfractions, three of which demonstrated only DNase activity while one subfraction hydrolyzed RNA faster than DNA. The serum of patients with many different autoimmune (AI) diseases contains small fractions of antibodies (Abs) interacting with immobilized DNA, which possess both DNase and RNase activities. Our data suggest that a fraction of abzymes from AI patients hydrolyzing both DNA and RNA can contain a subfraction of Abs against DNase I.
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PMID:Immunization of rabbits with DNase I produces polyclonal antibodies with DNase and RNase activities. 1844 84

The serum of patients with many autoimmune (AI) diseases contains small fractions of antibodies possessing both DNase and RNase activities. It was shown that immunization of rabbits with DNA, RNA, DNase I and RNase leads to production of antibodies with DNase and RNase activities. It is not known whether anti-idiotypic antibodies against DNase II can possess DNase or RNase activity. Electrophoretically and immunologically homogeneous polyclonal IgGs (pIgGs) from the sera of rabbits immunized with DNase II were obtained by sequential chromatography of the serum proteins on Protein A-Sepharose and gel filtration. It was shown for the first time that immunization of healthy rabbits with bovine DNase II produces IgGs with intrinsic DNase and RNase activities. IgGs from rabbits immunized with BSA or non-immunized animals were catalytically inactive. It was shown that approximately 10% of the total IgG DNase and RNase activities belong to anti-idiotypic antibodies to DNase II ( approximately 0.1% of total pIgGs), while 90% of the activities did not interact with Sepharose bearing antibodies against DNase II and might be antibodies to nucleic acids bound to DNase II. Affinity chromatography on DNA-cellulose using elution of antibodies with different concentration of NaCl and an acidic buffer separated catalytic IgGs into five antibody subfractions, three of which hydrolyzed RNA faster than DNA while two subfractions demonstrated only DNase activity. Our data suggest that a fraction of abzymes from AI patients hydrolyzing both DNA and RNA can contain subfraction of antibodies against DNase II.
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PMID:Immunization of rabbits with DNase II leads to formation of polyclonal antibodies with DNase and RNase activities. 1920 53

Chinese hamster ovary (CHO) cells are the host cell of choice for manufacturing biologic drugs, like monoclonal antibody, in the biopharmaceutical industry. Retrovirus-like particles (RVLPs) are made during the manufacturing process with CHO cells and it is incumbent upon the manufacturer to perform risk assessment based on levels of RVLP in unprocessed bulk. Quantification of RVLP using electron microscopy (EM) is the standard method. However, reverse transcription based real-time PCR (RT qPCR) is an alternative method available. This method involves RNase digestion of cell culture fluid to remove free RNA, followed by extraction of total nucleic acid and digestion with DNase to remove extracted DNA molecules, and then finally reverse transcription and PCR. Here we report a method where the nucleic acids extraction step is eliminated prior to qPCR. In this method the cell-free culture supernatant sample is digested with thermolabile DNase and RNase at the same time in a 96-well PCR plate; subsequently the enzymes are heat-denatured; then RT qPCR reagents are added to the wells in the PCR plate along with standards and controls in other wells of the same plate; finally the plate is subjected to RT qPCR for analysis of RVLP RNA in the samples. This direct RT qPCR method for RVLP is sensitive to 10 particles of RVLP with good precision and accuracy and has a wide linear range of quantification. The method has been successfully tested with different production batches, shown to be consistent, and correlates well with the extraction-based method. However, the results are about 1-log higher compared to EM method. This method simplifies the RVLP quantification protocol, reduces time of analysis and leads to increased assay sensitivity and development of automated high-throughput methods. Additionally, the method can be an added tool for viral clearance studies, by testing process-intermediate samples like Protein A column and ion-exchange column eluates, for increased confidence in purification of biologics manufactured in CHO cell culture.
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PMID:A direct RT qPCR method for quantification of retrovirus-like particles in biopharmaceutical production with CHO cells. 3269 2