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)

1. Pancreatic ribonuclease in dilute EDTA has been shown to condition rough-microsomal membranes from adult rat liver to accept exogenously added rat liver polyribosomes in vitro at 0-4 degrees C. Treated smooth membranes would not significantly interact with polyribosomes. 2. The conditioning process decreased the membrane RNA content and removed polyribosomes from vesicle surfaces as viewed electron-microscopically. 3. Binding to these conditioned membranes was shown to be uninfluenced by changes of temperature (0-37 degrees C) and pH (6.9-7.8) or the presence of cell sap, but was inhibited by increasing the concentration of potassium chloride. 4. Possession of a polyribosome-binding capacity by conditioned rough membranes was not dependent on adventitious materials that could be dislodged by high ionic strengths. 5. Trypsin treatment under mild conditions destroyed the binding capacity of ribonuclease-conditioned rough membranes. 6. A 2-10S residual RNA was recovered from ribonuclease-conditioned membranes, but its partial removal had no effect on the capacity of membranes to accept polyribosomes. However, some role for this residual RNA in attaching polyribosomes could not be discounted. 7. Evidence is considered that polyribosome-binding sites are intrinsic features of conditioned membranes isolated from rough-microsomal fractions, and that long-range ionic bonding is a primary factor in polyribosome interaction with these binding sites.
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PMID:The association in vitro of polyribosomes with ribonuclease-treated derivatives of hepatic rough endoplasmic reticulum. Characteristics of the membrane binding sites and factors influencing association. 515 23

The limiting factors of a cell-free system from rat brain for incorporating amino acids into protein were studied. The initial more rapid incorporation by microsomes, as opposed to that by ribosomes, is suggested to be due to damage of the ribosomes by detergent. The defect is rectifiable by incubation of the ribosomes in cell sap, so that ribosomes eventually incorporate more amino acid than do microsomes. This may be because ribonuclease, which is associated with the microsomes but removed by detergent treatment, inactivates the microsomal system. The factor that causes incorporation by microsomes to cease abruptly within 1h is not the lack of any precursor or of adenosine triphosphate, of the inactivation of cell-sap factors or the accumulation of inhibitory substances, but is a deficiency of usable messenger ribonucleic acid. Chain initiation in the system is negligible. Ribosomes also become jammed at the end of messenger ribonucleic acid molecules, unable to terminate protein chains. This eventually leads to jammed polyribosomes, which can be partially relieved by very low concentrations of puromycin. A study of the release of polypeptides synthesized in response to the addition of synthetic messengers did not provide any conclusive information on chain-termination sequences, but did indicate some phenomena that were artifacts. It is concluded that ribonuclease action is sufficient to account for all the deficiencies of the cell-free system, but a lack of chain initiation may be a contributory factor.
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PMID:The limiting factors of a cell-free protein-synthesizing system from rat brain. 541 23

1. After incorporation of [(14)C]valine in vitro, cerebral microsomes were separated into membrane-bound and free ribosomes by sucrose-density-gradient centrifugation. 2. In preparations from both 4-day-old and adult rats, free and bound ribosomes incorporated [(14)C]valine. Free ribosomes could be found as polysomes, which were highly active. 3. Microsomes labelled with [(14)C]valine in vitro were fractionated after deoxycholate treatment into a preliminary sediment, sedimented at 105000g (5min.), and ribonucleoprotein particles, sedimented at 150000g (70min.), to determine the role of membrane-bound ribosomes. In the adult the ribonucleoprotein particles retained most of the radioactivity, whereas in the young the preliminary sediment was as highly labelled as the ribonucleoprotein particles. 4. The labelled preliminary sediment from young preparations was both ribonuclease- and deoxycholate-resistant, and the nature of this material is discussed in terms of a possible structural component of microsomal membranes.
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PMID:Microsomal components in relation to amino acid incorporation by preparations from the developing rat brain. 603 14

1. The properties of enzyme activities hydrolysing the sulphate esters of dehydroepiandrosterone, oestrone and p-nitrophenol are reported. The preparation studied was obtained from the microsomal fraction of human placenta by ultrasonic treatment and addition of Triton X-100. 2. The behaviour of the preparation during sedimentation at 105000g and attempts at purification indicated that the activities were particulate. Electron microscopy demonstrated the rupture of vesicular structures approx. 0.5mu in diameter concurrent with the release of activity. 3. The three activities were always associated throughout repeated attempts at separation by sucrose-density-gradient centrifugation and Sephadex-gel filtration. On the basis of kinetic studies, stability studies and treatment with butanol and ribonuclease it was concluded that a separate enzyme is responsible for each of the three activities. Widely varying plots of activity as a function of pH were consistent with this conclusion. 4. On the basis of sensitivity of the enzymes hydrolysing dehydroepiandrosterone sulphate and oestrone sulphate to ribonuclease and sensitivity of all three enzymes to lipase, it was concluded that the three enzymes are bound to a particle containing lipid and RNA. Enzymic activity is dependent on structural integrity of the particle. 5. A spectrophotometric method for the assay of oestrone sulphate hydrolysis is described. 6. Hydrolysis of nitrocatechol sulphate by human placenta under conditions described for arylsulphatases A and B is reported.
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PMID:Properties of steroid sulphatase and arylsulphatase activities of human placenta. 606 Apr 47

Previous studies have established that 'informational molecules' present in cytoplasmic fractions of A. discoides may be transferred by microinjection into A. proteus. Clones derived from injected cells showed various changers, including lowered sensitivity to growth in streptomycin and neomycin, in which respects they resembled A. discoides. These changes in response to antibiotics were transferred independently and were permanent, the information being replicated over many generations. The most 'active' material in terms of the number of clones showing character changes was found following injection of 16S ribonucleoprotein obtained after sucrose density gradient centrifugation of the mcirosomal fraction. Polyacrylamide gel electrophoresis of the 16S material showed 3 small peaks of RNA. In order to obtain adequate amounts of material, these peaks of RNA were identified in electrophoresis profiles of RNA extracted from the whole microsomal fraction, and RNA eluted from these latter gels was injected into A. proteus. Although the number of surviving clones was low, all were examined for their response to growth in either streptomycin, neomycin, erythromycin or chloroquine. After injection of RNA eluted from the 3 small peaks of RNA (slices 26-33), 8 out of 10 and 9 out of 10 clones showed lowered sensitivity to growth in streptomycin and neomycin respectively, and resembled the donor A. discoides. No changes in responses to antibiotics were obtained from clones derived from cells injected with RNA eluted from another region of the gel, or after ribonuclease treatment of the RNA from slices 26-33. The relative molecular weights of these 'informational' RNA molecules were found to be between 9 and 13 X 10(4) Daltons.
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PMID:Evidence of low molecular weight RNAs involved in permanent character changes in amoebae. 615 21

Young rats were force-fed for 3 days a purified diet devoid of threonine and a number of aspects relating to RNA metabolism in the livers were studied. The findings in the livers of rats force-fed the threonine-devoid diet in comparison with those force-fed the complete diet were as follows: a) poly(A)-mRNA was increased in nuclei and in polyribosomes; b) DNA-dependent RNA polymerases I and II activities were increased; c) in vitro release of 14C-orotic acid labeled RNA from nuclei revealed that transport was unchanged and nucleoside triphosphatase activity of nuclear envelopes was unchanged; d) polyribosomes (total, free and membrane-bound) shifted toward heavier aggregation and in vitro 14C-leucine incorporation into protein was increased; e) RNase activities (at pH 5.4, 7.6, 9.5) were essentially unaltered; and f) in vivo 14C-choline incorporation into microsomal membranes was increased. By administering selected inhibitors of RNA and protein synthesis, such as actinomycin D, alpha-amanitin or cycloheximide, prior to killing the rats force-fed the threonine-devoid or complete diet for 3 days, it was demonstrated that the stimulatory effect on hepatic polyribosomes and protein synthesis in the experimental group was dependent upon new synthesis of poly(A)mRNA and of protein.
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PMID:Studies dealing with hepatic RNA metabolism in rats force-fed a threonine-devoid diet. 616 Feb 24

RNase-sensitive DNA polymerase activity (RSDP) was tested in different cell fractions of Neurospora crassa cell types and its morphological mutants. This RSDP was found localized in the microsomal pellet fraction and absent in the purified nuclear pellets isolated from different N. crassa cell types: conidia, germinated conidia, and mycelia. This enzyme is capable of synthesizing a DNA product only in the presence of all four deoxyribonucleoside-5' - triphosphates and Mg2+. Removal of RNA from the pellet fraction by RNase strongly inhibited the DNA synthesis. The endogenous synthesis of DNA in the microsomal pellet fraction was associated with the formation of an RNA:DNA hybrid as analyzed by Cs2SO4 equilibrium density gradient centrifugation. The DNA product after alkali hydrolysis hybridizes with the RNA isolated from the same pellet fraction, as analyzed by elution from hydroxylapatite column at 60C. This DNa product did not hybridize with poly (A). A few mutants tested showed this RNase-sensitive DNA polymerase activity.
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PMID:RNase-sensitive DNA polymerase activity in cell fractions and mutants of Neurospora crassa. 616 50

The subcellular RNA and protein metabolism have been studied in emetine-treated rats. Emetine treatment for a period of 10 days reduced the incorporation in vivo of [14C]-leucine into proteins of nuclear fraction of liver. This was accompanied by a reduction in the nuclear protein content. The mitochondrial fraction of heart exhibited an increase in the protein content after emetine treatment. This was, however, not accompanied by an increased rate of incorporation into its protein. On the other hand, the nuclear fraction of heart of emetine-treated rats showed a diminution in the rate of incorporation into its protein without having been reduced in protein content. The mitochondrial and microsomal RNA of liver and the microsomal RNA of heart responded to emetine treatment by showing increased levels. The liver RNase activity was reduced after emetine treatment, while the heart RNase remained independent of the treatment. It has been suggested that both synthesis and breakdown of liver proteins are reduced by emetine treatment. The synthesis of liver nuclear proteins was supposedly affected more than was its breakdown by emetine. The synthesis of rapidly turningover proteins of heart nuclear fraction and the catabolism of slowly turningover proteins of its mitochondrial fraction are thought to be reduced by the emetine treatment.
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PMID:Effect of emetine treatment on subcellular nucleic acid and protein metabolism. 618 17

Native bovine seminal ribonuclease is a dimeric protein, whose identical subunits (Mr 14500), linked through two disulfide bridges, can be dissociated by a selective reduction procedure. Evidence is presented that the synthesis in vitro, under reducing conditions, of bovine seminal RNAase, directed by polyadenylated RNA isolated from bull seminal vesicles (where the enzyme is synthesized in vivo), occurs in the form of a precursor, 18000-Da polypeptide. The precursor nature of this translation product was deduced by two criteria: (1) its specific immunoprecipitation with anti-bovine seminal RNAase antibodies; (2) its processing by dog pancreas microsomal membranes to produce a protein with a molecular weight similar to that of the subunit(s) of bovine seminal RNAase. Moreover, evidence is offered that the precursor polypeptide is able to form in vitro a dimeric molecule under conditions where no exogenous reducing agents were added.
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PMID:Bovine seminal ribonuclease precursor synthesized in vitro. 619 87

Bloodstream forms of Trypanosoma brucei have been screened for the presence of enzymes that could serve as markers for the plasma membrane, flagellar pocket, lysosomes, endoplasmic reticulum and Golgi apparatus in order to study the subcellular organization of the digestive system of the parasite. Acetylesterase, acid DNase, acid phosphatase, acid phosphodiesterase, acid proteinase, acid RNase, alanine aminotransferase, galactosyl transferase, alpha-glucosidase, inosine diphosphatase and alpha-mannosidase were partially characterized and their assays optimized for pH-dependent activity, linearity of reaction with respect to incubation time and enzyme concentration, and the effect of inhibitors and activators. The association of these enzymes with particulate material and the presence of structural latency were investigated. Acid proteinase and alpha-mannosidase are particle-bound and latent in cytoplasmic extracts; they can be activated and solubilized in part by Triton X-100. Similar results were obtained for acid phosphatase, acid phosphodiesterase and inosine diphosphatase. Neutral alpha-glucosidase, though partly sedimentable, does not show latency and is readily solubilized by the detergent. Galactosyl transferase is firmly membrane-bound even in the presence of 0.1% Triton X-100. Cell fractionation by differential centrifugation and density equilibration on sucrose gradients revealed that both alpha-mannosidase and acid proteinase are associated with organelles that band at a density of about 1.20 g/cm3. Inosine diphosphatase, galactosyl transferase, acid phosphatase and acid phosphodiesterase sediment predominantly as microsomal constituents equilibrating at densities between 1.13 and 1.15 g/cm3. In addition, inosine diphosphatase and galactosyl transferase exhibit considerable activity at higher densities (1.18-1.25 g/cm3). Neutral alpha-glucosidase is mainly recovered in the nuclear and microsomal fraction; its particulate part equilibrates as a single band at rho = 1.22 g/cm3. Acetylesterase and acid DNase are largely soluble, whereas acid RNase does not produce distinct sedimentation and banding profiles. In intact cells, neutral alpha-glucosidase and acid phosphatase appear to be highly accessible to their substrates. It is tentatively concluded that (a) acid proteinase and alpha-mannosidase are lysosomal enzymes, (b) acid phosphatase and acid phosphodiesterase are associated with the flagellar pocket and part of the former enzyme probably with the endoplasmic reticulum, (c) galactosyl transferase is a constituent of the Golgi apparatus, and (d) alpha-glucosidase may serve as a marker for the plasma membrane. Inosine diphosphatase may also be derived from the latter structure.
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PMID:Subcellular fractionation of Trypanosoma brucei bloodstream forms with special reference to hydrolases. 624 76


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