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)

By sequential acid treatment, gel filtration and KM-cellulose sorption a 18--20-fold purified preparation of ribonuclease with a yield of 50--60% was obtained from the culture liquid filtrate of Actinomyces rimosus 994. The preparation had a high specific activity of 450,000--600,000 units/mg protein, contained 85--98% protein, insignificant amounts of carbohydrates and hydroxytetracycline, and no quantities of DNase, phosphomonoesterases, phosphodiesterase or proteases. In RNA degradation (preparation of the total yeast RNA of the Sigma Co.) optimal results were obtained at 50 degrees C and pH 7.0--7.2 in phosphate buffer and 7.6--8.0 IN Tris-HCl buffer. The preparation was stable at high temperatures (80--100 degrees) in the wide pH range and during storage in the lyophilized form and in buffer solutions. RNase effect was inhibited by zinc, copper, iron and cobalt cations and activated by beta-mercaptoethanol, citrate and EDTA. Protamine sulphate and urea in low concentrations (0.01% and 1--4 M, respectively) accelerated and in high concentrations (1% and 8 M, respectively) terminated the enzyme reaction. With respect to many properties RNase from Act. rimosus 994 was similar to extracellular RNases, produced by other actinomycetes and fungi.
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PMID:[Preparation of extracellular ribonuclease form Actinomyces rimosus 994]. 3 16

The keratohyalin granules from 25 human oral leukoplakias, showing benign hyperorthokeratosis histologically, were examined employing a series of histochemical techniques. The tissues were fixed in 10% neutral buffered formalin, 80% methanol, or Carnoy's fluid. The keratohyalin granules stained intensely with Pauly's reagent, Congo red and Harris hematoxylin, indicating the presence of proteins. This was confirmed by abolishing the staining reaction by pretreatment with proteolytic enzymes. The keratohyalin granules also reacted with methyl green-pyronin by staining pink at their peripheries; this staining was abolished by pretreatment with ribonuclease, indicating the presence of ribonucleotides. The keratohyalin granules partially stained with toluidine blue and colloidal iron, indicating the presence of acid polysaccharides. The keratohyalin granules did not react with the Feulgen reagent, suggesting the absence of DNA. Our studies indicate that the keratohyalin granules in human oral leukoplakia are primarily protein(s) complexed with polyribonucleotides. The presence of a carbohydrate moiety suggests the possibility of a protein-polysaccharide component in the granules.
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PMID:Histochemistry of the keratohyalin granules in human oral leukoplakia. 5 23

In 56 patients with Hodgkin's disease, the following bloodtests were carried out: erythrocyte sedimentation rate (ESR), fibrinogen, alpha2-globuline, serium iron concentrations and alkaline phosphatase activity. In some patients we additionally measured alkaline leucocyte phosphatase and serum ribonuclease activity. In our series ESR, serum iron and alpha2-globuline concentrations were the most sensitive metabolic parameters. A rise in fibrinogen concentration, alkaline phosphatase and serum ribonclease activity seems to indicate extensive disease. It is not possible, however, to discern between a state of remission and stage I by means of these parameters. ESR, serum iron and alpha2-globuline concentrations might be either elevated or normal in both instances. These parameters seem important in order to distinguish between a remission or stage I on the one hand and extensive disease in stage III and IV on the other hand. Concomitant findings of ESR above 40 mmh, elevated concentrations of fibrinogen and alpha2-globuline, as well as elevated alkaline phosphatase and serum and serum ribonuclease activity mostly indicate stage III or IV.
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PMID:[Significance of metabolic parameters in Hodgkin's disease (author's transl)]. 5 79

It seems from the literature that colloidal iron (C.I.) binding sites on cell surfaces cannot be completely removed by treatment with Vibrio Colerae alpha-neuraminidase. We wondered if C.I. particles bind to negative groups other than the carboxyl groups of sialic acids. Using HeLa cells from suspension cultures and fresh human erythrocytes, we examined, with the transmission electronmicroscope, the influence of the following enzymatic and histochemical treatments on C.I. staining: alpha-neuraminidase; hyaluronidase; ribonuclease; alpha-amylase; mild methylation (MM); MM + saponification (Sap.); MM + Sap +MM; MM + Sap + alpha-neuraminidase; active methylation (AM); AM + Sap; AM + Sap + AM; AM + Sap + alpha-neuraminiadase; CH3OH (80%); Sap. It seemed from these experiments that the carboxyl groups of alpha-neuraminidase sensitive sialic acids constitute the majority of binding sites for C.I. to these particular cells. The most interesting candidates for the residual binding of C.I. are carboxyl groups of alpha-neuraminidase resistant molecules, sulfon, sulfin, and sulfate groups.
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PMID:Cytochemistry of colloidal iron binding to the surface of Hela cells and human erythrocytes. 6 32

Mouse 3T3, Simian virus 40 transformed 3T3 cells (SV3T3) and two SV3T3 lines showing reversion of their transformed phenotype (Rev 3 and Rev 5) have been studied with respect to electrophoretic mobilities and colloidal iron hydroxide (CIH) binding density visible by electron microscopy, before and after incubation with neuraminidase or ribonuclease. The results show that, in general, the marked changes in both sets of surface parameters associated with transformation are largely reversed in the Rev 5 revertant, and only partially reversed in the Rev 3 line. It was also observed that, in common with Ehrlich ascites tumor (EAT) cells examined previously, the densities of CIH-particles bound over the microvilli of all the cell types was 1.5 to 2.7 times higher than those bound to the spaces between them. In contrast to the EAT cells, the higher density of CIH particles bound over the microvilli was not due to neuraminidase-sensitive binding sites.
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PMID:Some electrical properties of the peripheries of murine 3T3 cells with respect to viral transformation and reversion. 17 59

This paper demonstrates the existence of regions in eight small globular proteins in which the side chains of sulfur-containing amino acids (cysteine and methionine) alternate in space with side chains of aromatic amino acids (histidine, phenylalanine, tryptophan and tyrosine). The proteins are: rubredoxin, high potential iron protein, cytochrome c, flavodoxin, deoxyhemoglobin, trypsin inhibitor, ribonuclease-S, and lysozyme. The sulfur-pi-bonded 'chains' involve a minimum of five and a maximum of 10 amino acids, and contain the most polarizable atoms within proteins. S-pi-chains give extra stability to the folding of proteins; they may also afford paths for the step-wise movement of electrons.
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PMID:Chains of alternating sulfur and pi-bonded atoms in eight small proteins. 20 19

We have investigated the pathogenesis of the polyclonal hypogammaglobulinemia associated with BALB/c plasmacytomas TEPC-183 and SPQC-11 to gain insight into the hypogammaglobulinemia observed in human myeloma. With pokeweed mitogen-driven IgM biosynthesis by mouse splenocytes as the indicator system for suppression, we found that a protein extract of asscites cells obtained from these tumor-bearing animals could suppress immunoglobulin production, whereas like extracts from a non-suppressing plasmacytoma, modified RPC-5, caused no suppression in vitro. Extracts of tumor ascites depleted of mononuclear phagocytes by iron carbonyl treatment showed little suppressor activity. The active extract was not cytotoxic and contained no mycoplasma or common murine viruses. Furthermore, the active suppressor factor appears to be a low m.w. protein that is not affected by treatment with ribonuclease. These results and others are consistent with the idea that the hypogammaglobulinemia of myeloma is due to the formation of immunoregulatory macrophage-like cells which synthesize a suppressor substance.
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PMID:Hypogammaglobulinemia in experimental myeloma: the role of suppressor factors from mononuclear phagocytes. 85 68

A method is described for purification of sulfhydryl oxidase from bovine milk which consistently yields preparations with greater than 3000-fold purification over skim milk. A concentration-dependent association-dissociation of the enzyme was adapted to the development of an isolation procedure. Purified preparations exhibited two zones, both of which displayed activity, upon polyacrylamide disc gel electrophoresis, but only one zone following disc gel electrophoresis in sodium dodecyl sulfate. Its mobility indicated a subunit weight of 89,000. Several lines of evidence suggest that iron is an integral part of the enzyme. Treatment of the enzyme with EDTA resulted in complete loss of activity which could be subsequently restored by dialysis against 1 muM ferrous sulfate. Furthermore, atomic absorption analysis and neutron activation analysis of separate enzyme preparations each indicated 0.5 atom of iron per subunit. Chemical analyses of sulfhydryl oxidase accounted for 97% of the sample weight, of which 89% could be attributed to amino acid residues and 11% to carbohydrate residues. Five half-cystine residues per subunit were indicated by cysteic acid analysis and by sulfhydryl group determination following reaction with sodium borohydride. Comparison of this value to the total sulfhydryl groups without reduction tentatively suggests the presence of one disulfide bond. Sulfhydryl oxidase was found to catalyze the oxidation of sulfhydryl groups in both small compounds and proteins, using O2 as oxidant and producing, in equimolar quantities, H2O2 and the corresponding disulfide. A Michaelis constant of 90 muM was obtained using reduced glutathione as substrate, under conditions of optimal pH and temperature, viz., pH 7.0 and 35 degrees. Substrate inhibition was apparent at GSH concentrations above 0.8 mM. In the presence of sulfhydryl oxidase, reductively denatured RNase was reoxidized and fully reactivated within 1 hour, whereas in the absence of the oxidase under otherwise identical conditions, full recovery of RNase activity required 24 hours. The presence of reducing agent was not required for this activity, nor was prior reduction of the sulfhydryl oxidase. Based on the observed activity, it appears that the enzyme could be involved in the biosynthesis of disulfide bonds in certain proteins.
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PMID:Isolation and characterization of sulfhydryl oxidase from bovine milk. 112 23

Natural killer (NK) and lymphokine-activated killer (LAK) cell cytotoxic functions can be strongly augmented by the iron-carrier protein lactoferrin (LF). LF significantly enhances NK and LAK activities when added at the beginning of NK or LAK cytotoxicity assays. LF is effective in augmenting cytotoxic activities at concentrations as low as 0.75 microgram/ml, and higher concentrations of LF induce greater augmentation of NK and LAK. Iron does not appear to be essential for LF to increase NK and LAK, as depleting iron from LF with the chelator deferoxamine does not affect the capacity of LF to increase cytotoxicity. LF is known to have RNase enzymatic activity, and LF enhancement of NK and LAK can be blocked by RNA. However, LFs from two different sources with over 100-fold difference in RNase activity are equally effective in enhancing NK and LAK. Furthermore, purified non-LF RNase does not modulate NK or LAK activity and DNA is as effective as RNA in blocking LF augmentation of NK or LAK cytotoxicity. Therefore, the RNase activity is unlikely to be responsible for LF enhancement of the cytotoxicities. Newborn infants are known to have low NK activity and NK and LAK cells have been implicated in host defense against microbial infections. Thus, maternal milk-derived LF may have a role in boosting antimicrobial immunity in the early stages of life. In adults, LF released from neutrophils may enhance NK and LAK functions in the inflammatory process induced by microbial infections.
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PMID:Modulation of natural killer and lymphokine-activated killer cell cytotoxicity by lactoferrin. 156 98

Interleukin-1 (IL-1 beta) increases the synthesis of both heavy and light (L)-ferritin subunits when added to human hepatoma cells (HepG2) grown in culture. RNase protection and Northern blot analysis with L-ferritin probes revealed that no changes in L-ferritin mRNA levels occur after cytokine stimulation. However, the induction coincides with an increased association of the L-subunit mRNA with polyribosomes. Since the recruitment of stored ferritin mRNA onto polyribosomes is seen when iron enters the cell, the effect of IL-1 beta on iron uptake was tested and was found to be unaffected by the lymphokine. Neither transferrin receptor mRNA levels nor the number of receptors displayed on the cell surface was affected by IL-1 beta. However, the action of the cytokine on ferritin translation is inhibited by the action of the intracellular iron chelator deferoxamine. These data indicate that IL-1 beta induces ferritin gene expression by translational control of its mRNA. The pathway of induction is different from iron-dependent ferritin gene expression whereas regulation requires the background presence of cellular iron.
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PMID:Translational control during the acute phase response. Ferritin synthesis in response to interleukin-1. 169 48


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