Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.27.5 (RNase)
 17,967 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Extracellular RNase N4 from Neurospora crassa is derepressible by limitation of any of the three nutrient elements obtainable from RNA. We have purified and characterized the enzyme from cultures grown under each of the three states of derepression. The purification procedure consisted of an ultrafiltration step, cation-exchange chromatography, and gel filtration. We found only one enzyme (N4) that hydrolyzed RNA at pH 7.5 in the presence of EDTA in culture filtrates from nitrogen-, phosphorus-, or carbon-limited cells. In all three cases, the enzymes were identical by polyacrylamide gel electrophoresis (Mr approximately 9,500) and by gel filtration (Mr approximately 10,000). There were no differences in thermal stability or pH optimum; all three cross-reacted with antibody to the nitrogen-depressed enzyme in interfacial ring and in Ouchterlony tests. Digestion of homopolyribonucleotides indicated that N4 preferentially cleaved phosphodiester bonds adjacent to guanine residues. Results indicate that the enzymes are very similar or identical and are probably products of the same gene. N4 appears to be homologous to guanine-specific RNases from other fungal sources.
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PMID:Characterization and comparison of a Neurospora crassa RNase purified from cultures undergoing each of three different states of derepression. 622 28

A new extracellular RNase, designated N4, was detected in culture filtrates from Neurospora crassa and its regulation was studied. Limitation of a nutrient obtainable from RNA alone was not sufficient to cause enzyme derepression. The addition of RNA to the medium had no inductive effect, but the addition of exogenous protein caused enzyme production. With protein in the medium, N4 was derepressible for all three elemental nutrients obtainable from RNA: carbon, nitrogen, and phosphorus. Successful carbon derepression required the addition of a small amount of proteolytic activity to the cultures, as has been reported for the carbon-derepressible proteases of N. crassa. Exogenous protein affected RNase production before translation. Effects of the exogenous protein appeared similar to those previously reported for N. crassa protease induction. N4 was under the control of the nit-2 and nuc-1 gene products. nit-2 and nuc-1 mutants were unable to derepress enzyme synthesis for nitrogen and phosphorus limitation, respectively; however, these mutants responded like wild types to the other two states of derepression. Enzyme synthesis was constitutive in the preg mutant. Results indicate that the transcription of the N4 structural gene responds to multiple regulatory gene products from different regulatory circuits and that external protein affects the synthesis of classes of hydrolases other than proteases.
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PMID:Regulation of a Neurospora crassa extracellular RNase by phosphorus, nitrogen, and carbon derepressions. 622 29

Insulin, ribonuclease, papain and collagen solutions saturated with nitrogen, N2O or air were irradiated with doses of 10 to 640 Gy of gamma rays. Protein solutions were also oxidized enzymatically in a system of horse-radish peroxidase: hydrogen peroxide. Column chromatography (Sephadex G-75 or Sephacryl S-200) of treated protein solutions revealed that they contain protein molecular aggregates. Nitrogen saturation of solution before irradiation was most favourable for radiation-induced aggregation of proteins. Fluorescence analysis of protein solutions resulted in detection of dityrosyl structures in irradiated as well as in enzymatically oxidized proteins. Concentration of dityrosine in proteins studied was determined fluorimetrically in their hydrolysates separated on BioGel P-2 column. In irradiated proteins, dityrosine was present almost exclusively in their aggregated forms. In proteins oxidized enzymatically, dityrosine was also present in fractions containing apparently unchanged protein. Mechanisms which could account for differences in the yield of dityrosine formation in radiolysis and in enzymatic oxidation of proteins are suggested.
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PMID:Radiolytic and enzymatic dimerization of tyrosyl residues in insulin, ribonuclease, papain and collagen. 633 34

A double-stranded ribonuclease has been purified more than 90-fold to near homogeneity from the yeast, Saccharomyces cerevisiae. The enzyme shows a high specificity for double-stranded RNA as its substrate. It has a molecular weight of 27000 as determined by sodium dodecyl sulphate/polyacrylamide gel electrophoresis. The enzyme degrades dsRNA optimally at 30 degrees C; it is stimulated by KCl and by the -SH reagent, dithiothreitol. In contrast to RNase III from Escherichia coli, the yeast enzyme is inhibited by divalent cations. Physiological studies have demonstrated that in vivo levels of the enzyme activity fell during the latter part of the exponential growth phase but rose during stationary phase. The specific activity of the enzyme in nitrogen-starved yeast cells was 2-3-fold higher than in non-starved cells. The enzyme could be detected in yeast strains containing both, one or none of the species of cytoplasmic dsRNA (L and MdsRNAs) and may, therefore, have some wider role.
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PMID:Purification and properties of a double-stranded ribonuclease from the yeast Saccharomyces cerevisiae. 636 60

Mammary gland polysomes are difficult to isolate from the lactating rat using methods developed for other species and tissues, most likely due to high calcium-stimulated ribonuclease activity in that tissue. A new method, utilizing ethyleneglycol-bis-(beta-aminoethylether)-N,N'-tetraacetic acid (EGTA) to bind calcium, yields highly aggregated polysomes from lactating rat mammary gland. Fresh mammary tissue is pulverized under liquid nitrogen. Free and membrane-bound polysomes are isolated by differential centrifugation in solutions containing 100 mM KCl, 100 mM MgCl2, 75 mM EGTA, 500 micrograms/ml heparin and 50 mM Tris buffer, pH 8.2 at 5 degrees C. Bound polysomes are released from the endoplasmic reticulum using Triton X-100 and deoxycholate. Polysome profiles are obtained on linear sucrose gradients and scanned at 254 nm. The method gives quantitative recovery of homogenate total RNA. To demonstrate that the method can be used to study nutritional effects on mammary gland polysome aggregation, lactating rats were fasted 22-66 h and then refed a stock diet for 71-95 h. Refeeding increased the percentage of polysomes (trimers or larger) in the bound fraction from 84 +/- 1 to 93 +/- 1% (P less than 0.001) and in the free fraction from 42 +/- 2 to 55 +/- 3% (P less than 0.001).
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PMID:A method for isolation of undegraded free and membrane-bound ribosomes from rat lactating mammary gland. 642 19

A complex of RNase A with a transition-state analog, uridine vanadate, has been studied by a combination of neutron and x-ray diffraction. The vanadium atom occupies the center of a distorted trigonal bipyramid, with the ribose oxygen O2' at the apical position. Contrary to expectations based on the straightforward interpretation of the known in-line mechanism of action of RNase, nitrogen NE2 of histidine-12 was found to form a hydrogen bond to the equatorial oxygen O8, while nitrogen NZ of lysine-41 makes a clear hydrogen bond to the apical oxygen O2'. Nitrogen ND1 of histidine-119 appears to be within a hydrogen-bond distance of the other apical oxygen, O7. Two other hydrogen bonds between the vanadate and the protein are made by nitrogen NE2 of glutamine-11 and by the amide nitrogen of phenylalanine-120. The observed geometry of the complex may necessitate reinterpretation of the mechanism of action of RNase.
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PMID:Active site of RNase: neutron diffraction study of a complex with uridine vanadate, a transition-state analog. 657 1

Serum levels of RNase activity, presumed to originate in the pancreas, have been suggested to be of use in the diagnosis of pancreatic cancer. We have used a radioimmunological assay of human pancreatic-like RNase to quantitate this protein in serum from normal blood donors and patients with a variety of diseases. Serum pancreatic-like RNase rises gradually with age, and its level is usually higher in males than females. Although many patients with pancreatic cancer show elevated serum levels of immunologically cross-reactive enzyme, others are apparently normal. In several other types of cancer, a similar pattern of elevated RNase is apparent. However, in kidney or bladder carcinoma and in patients with severe kidney disease, RNase levels are almost always greater than normal. Regardless of the nature of the disease, an elevated level of pancreatic-like enzyme is usually accompanied by above-normal levels of serum urea nitrogen. Hence, elevated circulating levels of pancreatic-like RNase are best related to kidney function and do not serve as a specific marker for cancers of the pancreas or other organs.
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PMID:Immunological assay of pancreatic ribonuclease in serum as an indicator of pancreatic cancer. 670 74

A method for radioimmunoassay of human pancreatic RNase was developed. The method is sensitive, reproducible, and specific. Almost no cross-reactivity exists between human pancreatic and liver RNases. A good correlation was observed between the serum concentration of pancreatic RNase as measured by radioimmunoassay and its enzymatic activity using polycytidylic acid as substrate. The concentration of serum pancreatic RNase correlates well with age, blood urea nitrogen, and albumin contents but does not correlate with serum amylase activity. Using the data of 52 patients with malignant tumors except pancreatic cancer, serum RNase level could be expressed by a multiple regression equation: Immunoreactive RNase content in pancreatic cancer was elevated in patients with complications from renal failure. Serum pancreatic RNase contents in patients with pancreatic cancer measured by radioimmunoassay agreed well with the values calculated using the equation derived from the data of patients with other malignant tumors.
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PMID:Radioimmunoassay for human pancreatic ribonuclease and measurement of serum immunoreactive pancreatic ribonuclease in patients with malignant tumors. 671 12

The effects of different intravenous nutritional regimens on a number of biochemical indices of nutritional status were studied during the 8-day period following severe trauma. The inclusion of large amounts of amino acids (high nitrogen (N) was shown to greatly improve N balance over an isocaloric regimen containing no amino acids (O g N). The concentration of serum albumin, transferrin, prealbumin, and retinol-binding protein all fell during the study period in both patient groups, whereas the serum concentrations of acute phase reactants and of ribonuclease increased in the two groups. The sum of plasma levels of branched-chain amino acids and the essential amino acids was increased to a greater extent in the high N group. These amino acid totals and the ratio of glycine/valine showed a significant correlation with N balance in this group. Despite the marked difference in N balance, 3-methylhistidine excretion was increased but equal in the two nutritional groups, suggesting an increased rate of muscle protein breakdown in both groups, which appears not to be influenced by amino acid nutrition. It is concluded that N balance can be significantly improved in the immediate posttrauma period by provision of amino acids together with energy substrates. None of the biochemical variables measured, with the exception of plasma levels of essential amino acids, reflected these marked differences in N balance.
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PMID:Biochemical changes associated with severe trauma. 677 18

Antiserum against the fibrogenesis controlling macrophage RNase was produced in rabbits. It caused an inhibition of 57% in the RNase activity in vitro. A distinct dose-response relationship was observed in the inhibiting effect of the antiserum on RNase-induced 3H-thymidine incorporation into cultured granulation-tissue fibroblasts. The antifibrogenic properties of the antiserum were also tested in vivo. Rat lungs were made silicotic by intratracheal administration of SiO2. This treatment clearly increased the following parameters: wet weight, DNA, RNA, nitrogen and hydroxyproline content of the lung tissue, and protein concentration, RNase activity, and cell count of the lung lavage fluid. Also, the RNase activity of the lavage fluid cells was increased. Periodical intratracheal administration of the anti-RNase antiserum, optimally at 1:1,000 dilution, decreased the DNA, RNA, and hydroxyproline content of the lung tissue, each by about 30%. The RNase activity of lavage fluid cells was decreased by about 60%. In conclusion the antiserum had no effect on the normal lungs, but it significantly suppressed the development of silicosis.
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PMID:Antifibrogenic effects of antiserum against the macrophage RNase. 683 34


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