Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.27.1 (RNase)
 16,360 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Low ionic strength (50 to 100 mM NaCl) and pH 6.0 were found to be optimal conditions for in vitro conversion of Epstein-Barr virus (EBV)-determined nuclear antigen (EBNA)-negative nuclei to EBNA-positive nuclei by addition of the complement-fixing (CF) antigen extracted from Raji cells. In vitro conversion of nuclei to EBNA-positively was sensitive to DNase but not to RNase treatment. This suggests that nuclear DNA is a specific target substance to which EBV-CF antigen binds. If nuclei were fixed with methanol/acetic acid and subsequently treated with 0.6 M NaCl, EBNA could be eluted from in vitro-converted Ramos nuclei with 0.3 and 0.4 M NaCl. The same conditions were also found to be optimal for the adsorption and elution of EBV-CF antigen in DNA-cellulose chromatography. This indicates that the DNA-binding properties of EBNA antigen can be studied by "chromatography" on fixed nuclei followed by the ACIF test. The obvious advantages of this method over chromatography on DNA-cellulose are its simplicity, the possibility of testing many samples in one experiment and, especially, the use of minimal amounts of material. Significant differences in elution patterns for EBNA were found when nuclei derived from different cell lines (Ramos, Raji, and P3HR-1) were converted in vitro to EBNA-positivity. EBNA is eluted from in vitro-converted nuclei of EBV genome-positive P3HR-1 cells at an almost 0.1 M higher concentration of NaCl than is necesssary for a similar degree of elution from nuclei of EBV genome-negative Ramos cells.
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PMID:Study of Epstein-Barr virus-determined nuclear antigen (EBNA) by chromatography on fixed cell nuclei. 8 40

Pseudomonas aeruginosa strain P15 produces not only pyocin R1 and phage PS10, but also a substance having a flexuous rod structure, the nature of which is so far unknown. A variant strain (P15--40) was obtained which produced these flexuous particles more effectively than the original strain, and the particles were purified to homogeneity and investigated. Several strains of P. aeruginosa were found to be killed by the particles. It was concluded that the flexuous rod-like particles are not related to pyocin R1 or phage PS10, but represent a new pyocin, which we have designated as pyocin F1. Pyocin F1 showed a different action spectrum and a different pattern on SDS-polyacrylamide gel electrophoresis from either pyocin R1 or phage PS10. The killing activity of pyocin F1 was of single-hit type. The activity was not affected by anti-R1, anti-R1-core or anti-PS10, or by DNase, RNase, pronase or trypsin, but was completely destroyed by treatment at 70 degrees C for 10 min. Some cofactor was required for the adsorption of this pyocin on sensitive bacteria. Another flexuous bacteriocin was also found and named pyocin F2.
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PMID:Biochemical properties of a new flexuous bacteriocin, pyocin F1, produced by Pseudomonas aeruginosa. 10 91

A polysaccharide antigen was isolated from Schistosoma mansoni egg homogenates by the phenol procedure. The crude preparation (CPEA) contained at least two antigens. The more purified antigen (PEA) was isolated by sequential enzymatic treatment of CPEA with DNase, RNase, Pronase, and alpha-amylase. PEA was resistant to boiling, freezing and thawing, mild acid and alkali, and chloroform, but was destroyed with periodate. It gave a positive reaction with anthrone reagent. PEA was eluted in the wash fraction from a DEAE cellulose collumn and in the void volume of a Sephacryl 200 column. After immunoelectrophoresis and polyacrylamide electrophoresis there was little or no migration. Amino acid analysis failed to reveal ninhydrin-positive material in the a hydrolyzate of PEA. These resluts suggested that PEA is a neutral polysaccharide with a m.w. of more than 200,000 and contains no amino acids or hexosamine. Antibodies against PEA were detected in sera obtained from mice infected with S. mansoni. PEA is different from previously described antigens derived from schistosome eggs.
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PMID:Isolation of a polysaccharide antigen from Schistosoma mansoni eggs. 10 42

The paper describes a method for isolating alkaline ribonuclease from the culture liquid Bacillus subtilis KP 349 which involved: submerged cultivation of the producer on complex and synthetic nutrient media with optimized RNase activity, acid treatment of the total culture liquid, and filtration through perlite. Further treatment may include either spray drying of the culture liquid filtrate or its concentration in a vacuum evaporator, dialysis of the concentrate against distilled water, and dialyzate lyophilization. As a result, commercial RNase preparations with activities of 30--60 thous. and 160--300 thous. units/g, respectively, were obtained. The enzyme purification was carried out by chromatography and rechromatography on phosphocellulose columns. The resultant RNase of Bac. subtilis had a specific activity of 41--44 thous. units/mg protein, contained no nonspecific phosphodiesterase, DNase, acid or alkaline phosphomonoesterases.
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PMID:[Preparation of extracellular ribonuclease from Bacillus subtilis]. 10 17

A human lung tumor-associated fetal antigen (LTFA) has been partially isolated and characterized. The antigen that differs in several immunochemical parameters from previously described lung cancer antigens was shared by fetal lung and liver tissue. The neoantigen migrated in immunoelectrophoresis as an alpha2-beta globulin, had an average molecular size of 7S, and was soluble in 50% saturated ammonium sulfate. Whereas LTFA was insensitive to both DNase and RNase treatment, its antigenicity was completely abolished by pronase. The biologic significance of this antigen and its possible clinical use were discussed.
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PMID:Partial characterization of a fetal lung antigen associated with human bronchogenic carcinoma. 10 44

Ribonucleic acid extracts of lymphoid cells from immune hosts were used to transfer in vivo and in vitro cell-mediated immune reactivity to a variety of antigens. The in vivo immune responses transferred by RNA included the delayed cutaneous hypersensitivity reaction to fungal and chemically-defined antigens and the tumor-rejection reaction to guinea pig hepatoma antigens. The in vitro immune responses transferred by RNA included macrophage migration inhibition by fungal, chemically-defined, and tumor antigens. The transfer activity of RNA preparations was contained in the 8 s to 18 s species of RNA and was sensitive to RNase but not to DNase or trypsin. Antigen was not detectable in the RNA preparations and appeared to have no role in the transfer activity. Syngeneic, allogeneic, or xenogeneic sources of RNA could transfer immune reactivity. In each system tested, the transfer of cell-mediated reactivity by RNA was specific for the antigen used to sensitize the RNA donor. The potential use of RNA-mediated transfer of immunity is discussed.
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PMID:Some perspectives on the transfer of cell-mediated immunity by immune-RNA. 11 79

A cytoplasmic component from group A streptococci produced complete suppression of human lymphocyte transformation induced by phytohaemagglutinin or the mixed lymphocyte reaction in vitro. It also suppressed antibody-forming cells in mice against sheep erythrocytes. The active substance was eluted as second and third fractions form Sephadex G-200 chromatography of the 100,000 g supernatant of sonically ruptured group A streptococci. The antimitogenic activity was not susceptible to trypsin, pronase, RNase or DNase digestion, but the activity was completely lost when it was sequentially digested, first with RNase and DNase and then with pronase. The active substance was not antigenic nor heat-labile at 56 degrees. It may be a protein component of a nucleoprotein.
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PMID:A potent antimitogenic factor from group A streptococci. 12 16

After lysis of Pseydomonas testosteroni with lysozyme and non-ionic detergents different DNA-protein complexes can be separated in 5-25% (w/v) neutral sucrose gradient. The protein to DNA ratio of these complexes varies between 0.5-4.5 to 1, whereby the faster sedimenting forms contain more protein than the slower sedimenting ones. Different initial rates of DNase digestion may indicate various degrees of DNA packing in these complexes. The chromosomal complexes of Pseudomonas testosteroni are relatively stable towards pronase. Treatment with RNase or sodium dodecylsulphate is accompanied by a dramatic increase in viscosity and decrease in relative density. It suggests that DNA in these complexes is maintained in its supercoiled form by RNA molecule(s) in a similar way as in isolated chromosome of E. coli.
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PMID:[Chromosomal structures of Pseudomonas testosteroni. I. Isolation and characterization of the chromosomal complexes. (author's transl)]. 13 46

KCl extract from rat kidney, rat liver, and Morris hepatomas inhibited [3H]thymidine incorporation into cultured cells. Tissues came from male inbred BUF rats. The most pronounced inhibition was achieved with the kidney extract. Protein synthesis was not inhibited during a 24-hour exposure of the cells to the inhibitor. Incorporation of [3H]deoxycytidine was inhibited, as was cell growth, when the kidney KCl extract was present for several days. [3H]thymidine incorporation was inhibited almost immediately after the addition of the extract. The inhibition was reversible. Regular [3H]thymidine incorporation was restored 24 hours after removal of the inhibitor, which was neither arginase nor a thymidine-degrading enzyme. The inhibitor was stable to heat (80 degrees C for 10 min) and resistant to trypsin, pronase, DNase, and RNase. Exposure of the extract to proteolytic enzymes, hyaluronidase, and neuraminidase resulted in a loss of inhibitory activity only after extensive dialysis of the treated extract. The inhibitor appeared to be a mucoprotein in which the carbohydrate moiety may be responsible for the inhibition. The KCl extract also inhibited RNA synthesis and DNA synthesis by the de novo pathway. The inhibition of phosphorylation of thymidine, however, appeared to be the primary action of the inhibitor.
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PMID:Inhibition of tritiated thymidine incorporation in cultured cells by rat kidney extract. 15 53

The binding of tritiated proesterone to the cytoplasmic progestogen receptors from oestrogen-primed sheep endometrium and myometrium has been investigated. The binding characteristics of the progesterone receptors from both sources were determined in the supernatant fractions obtained after high speed centrifugation of the myometrial and endometrial homogenates. High affinity binding proteins with identical association constants for progesterone (1 times 10-9 M-1) were detected in both endometrium and myometrium. The concentration of binding sites was also of the same order of magnitude in both tissues. After centrifugation on surcrose gradients, these binding proteins were shown to have similar sedimentation constants, 7S in a gradient containing no added KC1 and 4S in a gradient containing 0.4 M KC1. The binding peaks from both sources could be abolished by heating the cytosol at 60 degrees C for half an hour. The proteinaceous nature of the binding materials was demonstrated by incubation of the endometrial and myometrial cytosols with pronase, DNase and RNase: the binding was totally eliminated by the proteolytic action of pronase whereas DNase and RNase had no effect. The ligand specificity of the two progesterone binding proteins was studied using a competitive protein-binding technique. Both the endometrial and the myometrial receptor proteins were shown to bind only steroids which are known potent progestogens. In addition, the relative affinities of the binding proteins for 37 steroidal compounds closely resembled each other. Thus, the physiochemical and binding data obtained show that a very close similarity exists between the progesterone-binding proteins in the endometrium and myometrium of ovariectomized sheep after oestradiol treatment.
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PMID:Progesterone-binding proteins from endometrium and myometrium of sheep uterus: a comparative study. 16 95


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