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:3.1.27.1 (RNase)
16,360 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The factor(s) derived from fibrosarcoma-induced suppressor T cells was sensitive to pronase and neuraminidase, but not to trypsin, beta-galactosidase, DNase, or RNase. Protein and RNA, but not DNA, synthesis were required to mediate suppression. Suppressor T cell-derived factor(s) could be precipitated by a 50% saturated ammonium sulfate (SAS) solution. The 50% SAS fraction inhibited both in vitro and in vivo spleen cell blastogenesis, whereas the 80% and unprecipitated fractions had no inhibitory activity. Using Sephadex G-200 chromatography, the 2nd protein fraction (fraction II) contained an inhibitor of both DNA polymerases (IDP) and DNA synthesis (IDS) activity, which possessed no cytotoxic activity. In vitro DNA polymerase alpha activity was suppressed by fraction II, whereas DNA polymerase beta and gamma activities remained unchanged. Molecular weight of IDP/IDS, as determined by Sephadex G-200 gel filtration chromatography, was approximately 14,500. Attempts to separate IDP/IDS activities found in fraction II by anion-exchange chromatography and slab gel electrophoresis were not successful, which suggested that the 2 activities were the same or very similar molecules.
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PMID:Suppressor cell activity in tumor-bearing mice. III. Co-purification of a factor inhibiting cellular DNA synthesis and DNA polymerase activity. 645 73

Vaccination of mice with either Formalin-killed cells or cell extracts of a virulent strain and a weakly virulent strain of Vibrio vulnificus or with rabbit antisera (AS) against the Formalin-killed cells and cell extracts protected against the virulent strain of V. vulnificus. However, the virulent strain vaccines and AS elicited a significantly stronger immune response than the weakly virulent strain vaccines and AS. Adsorption of the AS with either the homologous or heterologous Formalin-killed cells significantly reduced the ability of the AS to protect mice. The major protective antigen(s) in the cell extracts migrated in the void volume of Sephacryl S-400 superfine, was not effectively sedimented by centrifugation at 100,000 X g for 2 h, had an isoelectric point of 3.8 to 4.2, and was sensitive to boiling or autoclaving for 15 min, periodate oxidation, and exposure to pH 12 but was resistant to 56 degrees C, trypsin, pronase, RNase, neuraminidase, and pH 4.5. Electron microscopy revealed that the virulent strain possessed a more dense ruthenium red-staining layer on its outer membrane and had a much smoother surface than the weakly virulent strain. Our results provide evidence that a major protective antigen and virulence factor of V. vulnificus is a heat-labile, acidic polysaccharide located on the bacterial surface.
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PMID:Protection of mice against Vibrio vulnificus disease by vaccination with surface antigen preparations and anti-surface antigen antisera. 646 46

A tumor-derived suppressor factor ( TDSF ) has been isolated from 3 M KCl extracts of a chemically induced fibrosarcoma of C3H/HeJ mice by preparative isoelectric focusing. Incubation of TDSF with normal spleen cells induces suppressor cells that enhance tumor growth and inhibit DTH to the chemical sensitizer 2,4-dinitro-1-chlorobenzene (DNCB). Similar suppressogenic activity has been detected in extracts of the 10T1/2 fibroblast line, an ultraviolet-induced fibrosarcoma of C3H/HeN mice, the C57B1/6J Lewis lung carcinoma, and four human colonic adenocarcinoma. TDSF activity was not found in extracts of syngeneic muscle or spleen cells. Chemical characterization of TDSF from the murine fibrosarcoma MCA-F revealed sensitivity to treatment with heat and RNase, partial sensitivity to treatment with trypsin, but resistance to treatment with DNase, pronase, and neuraminidase. TDSF has an apparent molecular weight of greater than 300 kDa by high-performance gel permeation chromatography. Acidic soluble factors isolated from murine and human tumors induce suppressor cells to inhibit cell-mediated immunity in an intact host.
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PMID:Soluble factors from murine and human tumors induce suppressor cells. 653 7

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

The presence of glycosaminoglycans (GAG) has been histochemically demonstrated in the CNS of various mammalian species. They have been related with some nerve functions as neurotransmitters storage and synaptic transmission. In the present paper, the histochemical properties of nerve cell cytoplasmic GAG were studied in several regions of adult human CNS. Samples of brain cortex, pons, upper medulla, and cerebellar cortex obtained by autopsy from subjects not dying after neurological diseases were fixed by immersion in glutaraldehyde, dehydrated with ethanol, and embedded in paraffin. The sections were stained with Alcian blue solutions adjusted to pH 2.5, 4.0, and 5.7. To the latter solution MgCl2 was added in increasing concentration from 0.05 to 1.2 M. Testicular hyaluronidase, neuraminidase, and ribonuclease were applied on simultaneous sections with their respective controls. The sequence of these reactions allowed us to demonstrate the presence of hyaluronic acid along chondroitin-4- and/or 6-sulphate in the cytoplasm of most nerve cells. The sulphated GAG showed certain variability in the various regions studied related specially with their grade of sulphation.
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PMID:Histochemical demonstration of cytoplasmic glycosaminoglycans in the macroneurons of the human central nervous system. 670 30

Oral cholera vaccine contains 45% of O-antigen (serovars Ogawa and Inaba in equal parts) and at least 9 serologically active proteins; of these, toxoid (about 60% of the total amount of protein) and 5 enzymes have been identified: neuraminidase, proteinase, ribonuclease, phospholipase and ATPase. The safety, absence of reactogenicity and definite immunological effectiveness of the preparation in the primary immunization of volunteers have been shown.
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PMID:[Biochemical and immunochemical characteristics of a new oral, chemical cholera bivalent vaccine and results of a trial of the preparation on volunteers]. 676 Jun 28

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

A human colony-stimulating factor (CSF)-producing cell line, T3M-5, has been established in vitro from a squamous cell carcinoma of the thyroid gland transplanted into athymic nude mice [congenitally athymic BALB/c (nu/nu) mice; Central Institute for Experimental Animals, Kawasaki, Japan]. Contaminating fibroblasts derived from a host nude mouse were eliminated by treatment with antiserum raised against nude mouse cells. T3M-5 cells have been continuously propagated during 3 years. The cells grew in a monolayered sheet with about 22 hours of population-doubling time and showed about 40% plating efficiency. The cells exhibited an epithelium-like morphology resembling the structure of the original tumor and showed tumor takes when inoculated into nude mice. Chromosome analysis revealed the cell line to be a human aneuploid line with a hypertriploid mode. The cells possessed the characteristic function of human CSF production in vitro and produced marked neutrophilia in tumor-bearing nude mice that were inoculated with the cultured cells. The molecular weight of the CSF was estimated at about 27,000 and was stable over the pH range 1.0-9.0 at 4 degrees C for 21 hours. The CSF activity was destroyed by either trypsin or chymotrypsin, but it resisted neuraminidase, DNase, and RNase. The cells could be well propagated in roller bottles. About 100 liters of the conditioned medium was obtained with the roller bottle culture method, which formed approximately 500,000,000 colonies of human bone marrow cells. The rate of recovery of CSF activity from the gel-filtration column was high (68.9%). This cell line is therefore expected to aid in the large-scale preparation of human CSF.
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PMID:Establishment and characterization of a human colony-stimulating factor-producing cell line from a squamous cell carcinoma of the thyroid gland. 698 94

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

Circulating M antigen, specific for genus Schistosoma, was previously described in serum, urine, patients' milk, and in serum and urine of animals infected by S. mansoni. The M antigen was thermostable and soluble in trichloroacetic acid. It was not hydrolyzed by protease, ribonuclease, amylase, or neuraminidase but destroyed by sodium metaperiodate. In the present study, we have purified the M ag by using trichloroacetic acid solubility, DEAE Sephadex, and immunoadsorption. The M ag showed a neutral electric charge, a m.w. heterogeneity, and was only stained by periodic acid-Schiff. The composition study revealed M ag was a glycoprotein with a polysaccharide moiety (63% of the molecules) particularly rich in galactose, fucose, glucosamine, and mannose, and with a high molecular ratio of serine and threonine. The presence of O-glycosidic linkage allowed M ag to be considered as a mucin or a mucus glycoprotein-like component. It was localized in the cell wall of the gut of adult worms.
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PMID:Purification, immunochemical, and biologic characterization of the Schistosoma circulating M antigen. 698 17


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