Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.26.9 (ribonuclease)
 6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

K562 human erythroleukemia cells can be induced to make hemoglobin by a variety of inducing agents. Most of these agents are effective in media supplemented with fetal bovine serum (FBS), but not in media supplemented with newborn bovine serum (NBS). The active factor in FBS has an apparent molecular weight of 30,000 daltons and appears to be a protein on the basis of the following properties: lability at 100 degrees C, inactivation by desferrioxamine plus trypsin, resistance to periodate, and resistance to ribonuclease. Media containing NBS can be used for induction if supplemented by either this factor or transferrin of bovine or human origin. The small size of the active factor (mol. wt. approximately 30,000 daltons) indicates that it is not identical to bovine transferrin (mol. wt. approximately 77,000 daltons). However, when iron-saturated bovine transferrin is digested with trypsin, the peptide fragments produced resemble the FBS factor in activity, size, and reaction with antibovine serum transferrin.
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PMID:K562 cell erythroid differentiation: requirement for a factor in fetal bovine serum. 392 91

Immunoenzymatic, clinical and follow up study of 3500 patients suffering from nervous forms of epidemic parotitis was performed. It is concluded that the adaptive humoral enzymes, ribonuclease and trypsin, the persistence of antigen to epidemic parotitis virus in CSF lymphocytes as well as the immunologic status of the patient at the disease onset play the leading role in the pathogenesis of its acute phase. It advisable to examine the factors enumerated in order to predict the clinical course of the disease. The treatment with adaptive enzymes was of great efficacy in 660 patients.
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PMID:[Various mechanisms of the pathogenesis and etiotropic therapy of neurologic forms of epidemic parotitis]. 398 4

The means by which coxsackievirus type A9 (CA9) is inactivated by proteolytic enzymes was investigated. After reaction of (14)C-leucine-labeled CA9 with Pronase, free leucine was liberated as measured by radiochromatography. Treatment of (14)C-leucine-labeled CA9 with trypsin or proteolytic filtrates of Pseudomonas aeruginosa caused the release of a variety of labeled substances. The extent of viral ribonucleic acid (RNA) release after exposure of CA9 to Pronase was determined by RNA infectivity tests or trichloroacetic acid solubility tests. Infective viral RNA was found not to be consistently released by reaction of CA9 with Pronase, but further treatment with 1% sodium dodecyl sulfate at pH 7.0 promoted viral RNA release. Sodium dodecyl sulfate treatment of CA9 that had not been reacted with Pronase did not inactivate virus or cause viral RNA release. Reaction of Pronase with (32)P-labeled CA9 resulted in the liberation of virus components soluble in cold trichloroacetic acid, whereas untreated CA9 or CA9 reacted with ribonuclease were precipitated by cold trichloroacetic acid. These results demonstrate that the primary means by which protease-sensitive enteroviruses are inactivated is by degradation of the virus capsid, with subsequent release of viral RNA.
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PMID:Degradation of coxsackievirus type A9 by proteolytic enzymes. 420 58

Infection of the bursa of Fabricius and chicken embryo fibroblast cell cultures with avian infectious bursal disease virus resulted in production of a number of virus-induced antigens. The antigens were specific, forming three precipitin lines by immunodiffusion with antiserum (designated PA-1, -2, and -3). To separate immunoprecipitin from the remaining viral particles, two (PA-1 and PA-3) were partially purified by subjection to two cycles of diethylaminoethyl-cellulose chromatography and filtration through a column of Sephadex G-150 gel. The precipitating antigen, PA-1, was found to migrate most slowly through the agar gel, remaining serologically active after treatment with heating (56 C for 1 h), trypsin, lipolytic solvents, deoxyribonuclease, and ribonuclease. Its density was 1.27 g/ml. Morphologically the antigen displayed a doughnut-shaped structure 8 to 12 nm in size. PA-3 migrated most rapidly through the agar gel. It was destroyed by treatment with heating and trypsin but not with lipolytic solvents, deoxyribonuclease, and ribonuclease. Density was about 1.25 g/ml. This suggests that the antigen is a part of viral structural components. PA-2 migrated through agar gel at a rate between that of PA-1 and PA-3. Because of its low concentration, PA-2 was not further characterized.
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PMID:Some properties of precipitating antigens associated with infectious bursal disease virus. 421 58

Australia antigen [Au(1)], a particle associated with viral hepatitis, was isolated from the plasma of a patient with chronic anicteric hepatitis and leukemia who had received radioactive phosphorus. We have found that the immunoreactivity and appearance of Au(1) in the electron microscope were not altered by treatment with enzymes including trypsin, pronase, lipase, phospholipase C, ribonuclease, deoxyribonuclease, amylase, and neuraminidase. In contrast, other serum constituents were degraded by these enzymes. Therefore, treatment of the patient's plasma with many enzymes was exploited as an initial step for the isolation of Au(1). Subsequently, Au(1) was purified from the enzyme-treated (32)P-labeled plasma by gel filtration through Sephadex G-200 and centrifugation through sucrose and in cesium chloride gradients. There were no detectable human serum components in the purest fractions, as tested by immunoelectrophoresis and immunodiffusion. The density of the purified Au(1) was 1.21 in CsCl. The particle measured about 200 A in diameter, was predominantly spherical in shape and appeared to be composed of subunits. Nucleic acids were not detected by spectrophotometric, radiochemical, and chemical analyses. Immunoreactivity of purified Au(1) was destroyed by heating for 1 hr at 85 degrees C but was stable at 56 degrees C. Treatment with Carnoy's solution (3 parts ethanol:1 part glacial acetic acid) followed by pronase disrupted the particles as seen with the electron microscope. These findings, combined with other published information on Australia antigen and viral hepatitis, suggest that the bulk of Australia antigen in the blood of this patient is an incomplete virus or virus capsid.
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PMID:Australia antigen (a hepatitis-associated antigen): purification and physical properties. 424 40

Synthesis of collagen on polyribosomes has been demonstrated in vitro in chick embryo corium by radioisotope incorporation, zone centrifugation through sucrose gradients, and analytical ultracentrifugation. Collagen synthesis was associated with polyribosomes ranging in size, as reflected by their sedimentation constants, from about 180S to approximately 1600S. Most of the newly formed collagen, hydroxyproline, was present on the largest polyribosome aggregates ( approximately 350-1600S), but small polyribosomes ( approximately 180-200S) also contained collagen. On the basis of the proline-(14)C/hydroxyproline-(14)C ratios and the disrupting effect of collagenase, the proposal is made that the 350-1600S polyribosomes from this tissue are involved predominantly in collagen synthesis. The large polyribosomes are disrupted extensively by collagenase but only partially by ribonuclease and trypsin. Therefore, it appears that they are stabilized by the interaction of newly forming collagen chains. Evidence is presented consistent with the hypothesis that these large polyribosomes are formed by the aggregation of small polyribosomes (180-200S) through the interaction of collagen polypeptides. It is suggested that these small polyribosomes might be involved in the synthesis of subunits of the collagen alpha chain.
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PMID:Biochemical and physicochemical characterization of collagen-synthesizing polyribosomes. 429 67

Physicochemical and immunological techniques have been used in an attempt to characterize a filterable agent, separated from the intestines of mice raised under ordinary conditions of husbandry, which produces a lasting depression of weight in specific pathogen-free (SPF) mice when administered to them orally shortly after birth. Although this agent has not yet been identified, it will be tentatively designated here as enterovirus. The mouse enterovirus can be readily sedimented by ultracentrifugation and by precipitation at pH 4.3; it does not pass through cellophane membranes. Its infective power is completely destroyed by ultraviolet radiation, but is resistant to heating at 56 degrees C, exposure to ether, treatment with trypsin, ribonuclease, and deoxyribonuclease. Dialysis and treatment with ether and nucleases greatly increase the infective activity of the intestinal filtrates containing the enterovirus, a finding which suggests that these procedures eliminate or destroy some inhibitory substance(s). The mouse enterovirus causes hemagglutination of mouse red blood cells. When injected into rabbits, it elicits in them an immune response that renders their serum capable of neutralizing its weight-depressing activity. As measured by inhibition of hemagglutination or complement fixation, the sera of infected mice do not exhibit any significant activity against usual mouse viruses. Centrifugation of the mouse enterovirus in 50%-20% sucrose gradient gave almost complete recovery of the infectivity and of hemagglutinating activity in the same fraction. In contrast, the protein content of the material was distributed through the various fractions. Consequently, this procedure resulted in a marked increase of specific activity.
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PMID:Lasting biological effects of early environmental influences. IV. Notes on the physicochemical and immunological characteristics of an enterovirus that depresses the growth of mice. 431 May 4

Poliovirus type I LSc strain labeled with (14)C-uridine was adsorbed onto isolated plasma membranes and incubated with them. When membranes from Hep-2 or Vero cells were used, 22% of the label was converted to a trichloroacetic acid-soluble form, when trypsin or ribonuclease was added, the fraction rendered soluble was increased, and when the two enzymes were added in sequence, 85% or more of the label became trichloroacetic acid-soluble. This labilization of poliovirus could be reproduced when butanol-solubilized proteins from membranes were substituted for the whole plasma membranes, but it did not occur with membranes from polio-virus-resistant calf kidney or BHK-21 cells.
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PMID:Uncoating of poliovirus by isolated plasma membranes. 431 52

1. During the action of mescaline sulphate on goat brain-cortex slices the ribosomal particles become susceptible to breakdown, releasing protein, RNA, acidsoluble nucleotides and ninhydrin-positive materials, resulting in loss of ribosomal enzyme activities. 2. Ribosomes of the mescaline-treated cortex slices undergo rapid degradation in the presence of trypsin and ribonuclease. 3. Mescaline does not alter the chemical and nucleotide compositions or the u.v.-absorption characteristics of ribosomal particles, however.
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PMID:Mescaline-induced changes of brain-cortex ribosomes. Effect of mescaline on the stability of brain-cortex ribosomes. 431 16

Concentrations of the synthetic polymer polyriboinosinic.polyribocytidylic acid that produced no detectable toxicity in normal L cells produced marked cytotoxicity in L cells treated with interferon. This increase in the susceptibility of cells to the toxicity of the polymer was also observed in human cells and secondary mouse embryo cells treated with homologous interferons before exposure to the polynucleotides. The degree of enhancement of toxicity was dependent on the concentration of interferon to which the cells were exposed. The ratio of antiviral activity induced by interferon to enhancement of toxicity by interferon remained constant through about 1000-fold purification. Various interferon preparations induced by viruses or by polyriboinosinic.polyribocytidylic acid in vivo or in vitro, and international reference standard interferons all exhibited enhancement of toxicity. Both enhancement of toxicity and antiviral activity were destroyed by trypsin and by incubation at 56 degrees for 1 hr, did not act on heterologous cells, were not sedimented by ultracentrifugation, and were not inactivated by ribonuclease, deoxyribonuclease, irradiation with ultraviolet light, or exposure to a pH of 2.
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PMID:Increased susceptibility of cells treated with interferon to the toxicity of polyriboinosinic-polyribocytidylic acid. 450 64


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