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:3.1.27.5 (RNase)
17,967 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A method for electrophoretic concentration of differently charged proteins is described. A nonlinear pH gradient is generated by imposing a potential gradient on an electrolyte system composed of (+)H3PO4-valine (pI 6.0)-Servalyte (pH 9-11)-triethylamine(-). Proteins contained in the valine solution accumulate at the interphase formed between the valine solution and the Servalyte solution. This interphase acts as a barrier or liquid membrane to all proteins having isoelectric points in the range 6-9. For proteins having isoelectric points in the range 5-7 valine is replaced by histidine (pI 7.64) and the Servalyte by Pharmalyte, pH 2.5-5.0. Ribonuclease, hexokinase, bovine serum albumin, and hemoglobin were concentrated and recovered from the top of the column using a peristaltic pump. The duration of concentration process was 1-4 h, the length of the run depending on the experiment scale (20 or 100 ml protein solution), the amount of protein, and the isoelectric point of the protein. Proteins were concentrated 9- to 48-fold, depending on the initial volume and concentration of the protein. The recoveries ranged from 79.7 +/- 1.1 for hemoglobin to 93.17 +/- 2.84 for ribonuclease.
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PMID:Electrophoretic concentration of proteins in a nonlinear pH gradient. 673 3

Ribonuclease F1, the guanine-specific ribonuclease of Fusarium moniliforme, was purified to homogeneity by a combination of ethanol fractionation, affinity chromatography and DEAE-cellulose column chromatography. The adsorbent for the affinity chromatography was synthesized by the coupling of periodate-oxidized guanosine 5'-monophosphate to aminohexyl agarose followed by sodium borohydride reduction. Ribonuclease F2, the minor component, was also purified to near homogeneity by the same procedure. Ribonucleases F1 and F2 had the same molecular weight (about 11,000) as determined by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. They also showed the same amino acid composition and differed only in the isoelectric point: 4.10 for F1 and 3.96 for F2.
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PMID:Purification by affinity chromatography and physicochemical properties of the guanine-specific ribonuclease of Fusarium moniliforme. 678 May 47

The three-dimensional structure of Ribonuclease St (RNase St), the extracellular ribonuclease from Streptomyces erythreus, has been deduced based on a preliminary electron density map at 2.5 A resolution. RNase St has a substrate specificity similar to ribonuclease T1 which catalyzes the splitting of the phosphodiester bond of guanylic acid. Crystals grown as diamond plates have space group C2 with unit cell parameters a=88.4, b=33.0, c=69.0 A, beta = 98.4 degrees having two enzyme molecules per asymmetric unit. Phases were obtained by use of KAu(CN)4, phenylmercuric acetate and UO2 (CH3COO)2. The overall dimensions of the molecule are 40 X 30 X 25 A. The most prominent secondary structural features are two turns of alpha-helix and a three strand stretch of antiparallel beta-sheet. The alpha-carbon backbone of RNase St seems to have no apparent correlation with that of ribonuclease A.
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PMID:Preliminary crystal structure analysis of a microbial, guanine-specific ribonuclease St at 2.5 A resolution. 679 45

Ribonuclease A was introduced into the cytoplasm of IMR-90 human diploid fibroblasts by red cell-mediated microinjection. Early passage fibroblasts degraded ribonuclease A with a half-life of approximately 90 h in the presence of 10% fetal calf serum and enhanced the degradative rate 1.6-fold upon serum withdrawal. Senescent cells degraded ribonuclease A more slowly with half-lives ranging between 125 and 250 h and had diminished capacities to enhance the catabolism of this protein during serum starvation. Decreased protein degradation in senescent cells was also evident for microinjected RNase S-protein, RNase B, aldolase, lysozyme, and the synthetic copolymer polyglutamate: tyrosine:alanine (1:1:1). These alterations in the mechanisms and regulation of intracellular protein degradation may contribute to several biochemical abnormalities characteristic of aging cells and organisms.
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PMID:Altered degradation of proteins microinjected into senescent human fibroblasts. 717 58

There are indications that exocrine pancreatic enzymes may undergo an enteric recirculation. Ribonuclease (RNase) is present in considerable quantities in pancreatic exocrine secretions. Therefore we studied the intestinal transport of pancreatic RNase using everted gut sacs from duodenum, midgut, and ileum of young rats. Gut sacs were incubated aerobically at 37 degrees C, 22 degrees C, and 0 degrees C, and anaerobically at 37 degrees C. Measurable amounts of RNase crossed the intestinal barrier, but neither duodenum, midgut nor ileum absorbed RNase preferentially. The experimental data favor simple diffusion of RNase across rat small bowel. However, the amounts of pancreatic RNase absorbed were small. Thus, while our data do not negate the concept of an enteropancreatic recirculation in the rat, only a minor quantity of luminal, pancreatic RNase could recirculate.
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PMID:Permeability of adolescent rat intestine to pancreatic ribonuclease. 718 37

The degradation of S--S bonds in 0.2 M-NaOH at 25 degrees C was studied for a series of proteins and simple aliphatic disulphide compounds, by using cathodic stripping voltammetry, ion-selective-electrode potentiometry, spectrophotometry and ultrafiltration. The disulphide bonds that dissociated in 0.2 M-NaOH were usually those that are solvent accessible and that can be reduced by mild chemical reductants. Some unexpected differences were found between similar proteins, both in the number of S--S bonds dissociated and in their rates of decomposition. Chymotrypsin has one S--S bond attacked, whereas chymotrypsinogen and trypsinogen have two. Ribonuclease A has two S--S bonds dissociated, but ribonuclease S and S-protein have three. Denaturation in 6 M-guanidine hydrochloride before alkaline digestion caused the loss of an additional S--S bond in ribonuclease A and insulin, and increased the rate of dissociation of the S--S bonds of some other proteins. The initial product of S--S bond dissociation in dilute alkali is believed to be a persulphide intermediate formed by a beta-elimination reaction. This intermediate is in mobile equilibrium with bisulphide ion, HS-, and decomposes at a mercury electrode or in acid solution to yield a stoichiometric amount of sulphide. Rate constants and equilibrium constants were measured for the equilibria between HS- and the intermediates involved in the alkaline dissociation of several proteins. Elemental sulphur was not detected in any of the protein digests. It is suggested that formation of HS- from a persulphide intermediate involves a hydrolysis reaction to yield a sulphenic acid derivative. The small polypeptides glutathione and oxytocin gave only a low yield of persulphide, and their alkaline decomposition must proceed by a mechanism different from that of the proteins.
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PMID:Degradation of protein disulphide bonds in dilute alkali. 721 43

Ribonuclease isolated from human urine is a glucoprotein of molecular weight 33,000. The purified enzyme inhibits: (1) the stimulation of 3H-thymidine uptake into lymphocytes by phytohemagglutinin, pokeweed, and concanavalin A; (2) the growth of pancreatic fibroblastoid cells in in vitro cell culture, and (3) the growth of colonies in bone marrow cell cultures. Ribonuclease levels in the uremic patient vary from 9,500 to 35,000 U/ml (normal 1,041 +/- 247). Serum ribonuclease levels are unaffected by dialytic procedures. It is suggested that the ribonuclease glycoprotein may represent a large number of nondialyzable high molecular weight uremic 'toxins'.
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PMID:Ribonuclease activity in renal failure. Evidence for toxicity. 726 14

Ribonuclease activity in the serum of patients with histologically confirmed ovarian carcinoma is significantly higher than in serum of patients with benign tumors of the ovary and that of healthy controls. In 847 samples collected during a period of 20 months the course of the ribonuclease activity of 41 patients receiving cytostatic treatment was determined. The ovarian carcinoma of all 41 patients was histologically ascertained. Three typical examples are presented.
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PMID:[Serum ribonuclease activity in gynecologic neoplasms. The behavior of serum ribonuclease in ovarian cancer under cytostatic therapy]. 746 46

Ribonuclease Inhibitor (RI) has been purified from pig testis. It contains 30 half-cystines whose oxidation affects its ability to bind and inhibit ribonuclease (RNase). By N-terminal sequence analyses testis RI showed to be identical to that from porcine liver, for which a characteristic all-or-none type of SH-oxidation by 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) has been reported (Fominaya, J.M., and Hofsteenge, J. (1992) J. Biol. Chem. 257, 24655-24660). Under comparable reaction conditions, testis RI bound to RNase A did not exhibit this particular type of oxidation; instead, bound RI got intermediate oxidation degrees (up to 14 thiols oxidized per RI moiety) without dissociating from RNase. Moreover, RNase bound to partially oxidized RI was able to express some (15%) of its potential activity (active complex). Only when DTNB treatments accounted for complex dissociation (> 14 thiols oxidized per RI moiety) the released RI molecules exhibited the all-or-none oxidation behavior. By both kinetic and circular dichroism analyses, conformational changes have been evidenced for the transition from the inactive to the active form of RI-RNase complex. Relaxation of RI-RNase binding without major alterations in RI structure is proposed as responsible for complex activation. The results are discussed in terms of a model for the reversible regulation of RNase activity mediated by the redox status of RI.
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PMID:Thiol-disulfide exchange of ribonuclease inhibitor bound to ribonuclease A. Evidence of active inhibitor-bound ribonuclease. 749 72

An evaluation of the analytical performance of a method for determining ribonuclease catalytic activity employing digestion of RNA substrate was made. It was found that the relationship between concentrations of ribonuclease standards and concentrations of the reaction products, expressed as the 260 nm light absorbance values, was nonlinear and fulfils a binomial function. Substituting ribonuclease activities by square roots of ribonuclease activity values, a linear relationship with light absorbance values, ranging from 0.08 to 0.400 was obtained. In the present work one unit of ribonuclease catalytic activity was defined as RNA-degrading activity which in the assay conditions caused A260 equal to 0.332. The general equation of the ribonuclease catalytic activity was: Ribonuclease (U/l) = [(A260 - 0.02)/0.316]2. In spite of the nonlinearity of the standard curve, the actual CV values did not depend essentially on the value of measured activity and were estimated as 13%.
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PMID:Assessment of a method of determining ribonuclease activity employing RNA as substrate. 752 6


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