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)

It is found, that the protein content in chloroplasts remained constant in conditions of drought, while RNase activity in chloroplasts was decreased in 2-2.5 times as compared with total leaves and hyaloplasma. No reliable differences in base composition of DNA and RNA were found in cotton variety "Tashkent 2" under the lack of water.
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PMID:[Activity of chloroplast RNase under drought]. 91 35

Steady state inactivation data on dilute aqueous solutions of RNase show that all water radicals, e-aq, OH, and H are responsible for the inactivation, but the most efficient radical is H atom, only about 4 of them being required for one inactivating event. The data are, therefore, more in agreement with the conclusions of Mee et al. (1972). In the transient absorption spectra of pulse irradiated ribonuclease different components derived by the individual radicals are observed. Organic and inorganic selenium-containing compounds offer a great protection of the enzyme activity, in agreement with the data obtained in other chemical and biological systems. In particular the effects of two new secondary radicals (CNSe)-2 and SeO-3 are in good accord with the known structure of ribonuclease.
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PMID:Further investigation on the radiation induced inactivation of ribonuclease and the radioprotective effect of some selenium-containing compounds. 92 59

The effects of a combination of an alcohol and urea on the transition temperature of bovine ribonuclease were investigated. The combined effects on the transition temperature of ribonuclease of a polyvalent alcohol and urea are about equal to the algebraic sum of the effects of each individual additive. The effects of a monovalent alcohol and urea are not cummulative, especially not at low temperatures (30 degrees C). The presence of urea decreases the hydrophobic effect of a monovalent alcohol, strongly at low temperatures, to a lesser degree at high temperatures (60 degrees C). Consequently, urea hinders the interhydrophobic interactions by affecting the water molecules.
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PMID:The effects from combining urea and an alcohol on the heat-induced reversible denaturation of ribonuclease. 94 44

O antigen extracted from whole cells of Bacteroides fragilis ss. fragilis NCTC 9343 with 45 per cent aqueous phenol has been purified by gel filtration and chromatography. First, the water phase was treated with RNase and DNase and passed through a column of agarose. The chromatographic procedures included ion exchange on a column of DEAE-cellulose and adsorption to hydroxylapatite. The O antigen was eluted from the DEAE-cellulose with a gradient of NaCl, and from the column of hydroxylapatite with 1 M phosphate buffer, pH 6.8. Inhibition of indirect haemagglutination was used to detect the O antigen in the eluates.
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PMID:Purification of the O antigen of Bacteroides fragilis ss. fragilis NCTC 9343 from phenol-water extracts by gel filtration and chromatography on deae-cellulose and hydroxylapatite. 96 34

The present paper describes intracellular changes in ribonuclease specific activity during Ca2+-induced sporangium formation in the water mold Achyla bisexualis. The enzymes undergo a decrease in activity prior to crosswall formation followed by an increase in activity during spore cleavage. As spore discharge occurs the RNase activity again decreases. A large percentage of the nuclease activity is associated with a lysosomal-like fraction of the cell, but there is also considerably activity associated with nuclear and microsomal fractions. Addition of cycloheximide or actinomycin D at various times during development prevents further decrease or increase in the enzyme activity. Mixing of cell extracts from different developmental stages provides evidence that inhibitors or activators of the enzyme activity are not responsible for the activity levels evident at the different stages. There is a change in the total levels of presumptive mRNA during Ca2+-induced sporangial formation which appears to be associated with the patterns of RNase activity. Utilizing total cellular RNA and Poly(A)+ RNA with the crude ribonuclease preparations, no substrate specificity could be ascertained.
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PMID:The development patterns of lysosomal enzyme activities during Ca2+-induced sporangium formation in Achyla bisexualis. III. Ribonucleases. 98 98

The hydroxyl groups of poly(ethyleneglycol) have been esterified (partly) with a number of carboxylic acids. When these esters are included in dextranpoly(ethyleneglycol)-water biphasic systems the partitions of proteins and membranes between the two phases (and the interface) are in some cases strongly affected. The affinity of serum albumin for the poly(ethyleneglycol)-rich phase is strongly increased when the fatty acid group consists of more than 10 carbon atoms. The partition also depends on the number of double bonds in the fatty acid. A corresponding relationship is found for membranes from spinach chloroplasts. The partitions of ovalbumin, lysozyme (EC 3.2.1.17) and ribonuclease (EC 3.1.4.22) are not influenced by the fatty acid esters. Esters of dibasic carboxylic acids show a minute but marked effect on the partition of proteins in general while malate and tartrate esters affect strongly the partition of chloroplast membranes. The partitions of both proteins and membranes are influenced by poly(ethyleneglycol) deoxycholate. Experiments with malate dehydrogenase (EC 1.1.1.37), lactate dehydrogenase (EC 1.1.1.27), fumarase (EC 4.2.1.2), enolase (EC 4.2.1.11) and glutamate-ocaloacetate transaminase (EC 2.6.1.1) show that their partitions, measured on enzymic activity basis, is changed when esters of benzoic, linolenic, tartaric or deoxycholic acid are included in the biphasic system. The mechanism behind the effect of the esterified poly (ethyleneglycol) on the partition of biomaterial, in this type of aqueous biphasic systems, is discussed in terms of a direct binding of the esters to the partitioned material.
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PMID:The effect of poly(ethyleneglycol) esters on the partition of proteins and fragmented membranes in aqueous biphasic systems. 99 68

Cytidine and 4-N-acetylcytidine were compared as phosphate acceptors in dinucleoside monophosphate synthesis catalyzed by pancreatic ribonuclease with uridine-2',3'-cyclophosphate and cytidine-2',3'-cyclo phosphate as phosphate donors. Because of low solubility of 4-N-acetylcytidine in water, the synthesis was carried out in aqueus-organic media. The results obtained indicate that acetylation of the exoaminogroup of cytidine decreases its acceptor activity. For the first time uridilyl-(3'-5')-4-N-acetylcytidine and cytidilyl-(3'-5')-4-N-acetylcytidine are prepared enzymatically by pancreatic ribonuclease.
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PMID:[Acceptor activity of 4-N-acetylcytidine in the synthesis of (3'-5')-internucleotide bond catalyzed by pancreatic nuclease]. 102 91

The bone inducing factor derived from BF osteosarcoma was purified in the following manner. Step 1. The sarcoma, grown in CBA mice, was excised and lyophilized. Step 2. The powder was washed with chilled acetone. Step 3. The acetone-treated powder was then homogenized with chilled distilled water. Step 4. Washing with 0.15M KCl. Step 5. The precipitate was incubated in in 0.2 N NH2OH, pH7.0, for 48 H at 25 degrees. After Step 5, the bone-forming activity showed a slight increase; however, the factor remained insoluble. The properties of the factor were as follows. The factor is relatively relatively heat stable; the osteogenic activity survived the treatment at 75 degrees for 15 min or at 55 degrees for 19 h. The activity was easily lost by mechanical shaking. Incubation with DNase, RNase, neuraminidase, chondroitinase ABC and beta-galactosidase left the osteogenic activity intact, but treatment with either pronase or collagnease destroyed this activity. The results suggest that the factor may be a protein. The activity was seen with the lyophilized BF osteosarcoma cells (without matrix), and it is probable that the factor was exclusively synthesized in the cells. The bone formation, observed across a millipore filter when living BF osteosarcoma enclosed in a millipore chamber was implanted in mice, suggests the synthesis and secretion of the factor from the cells.
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PMID:Studies on a factor responsible for new bone formation from osteosarcoma in mice. 105 58

The conformation of zein, a seed protein from corn, was determined by optical rotary dispersion measurements in a wide variety of nonaqueous solvents. Over a wide range of dielectric constants, in pure and mixed solvent systems, the helical content was independent of dielectric constant. Determination of the helical content of insulin and ribonuclease in several of these solvents indicated a variation in secondary structure comparable of that of zein. Though virtually insoluble in water, zein not only is a globular protein in nonaqueous solutions, but has conformational properites characteristic of more conventionally behaving globular proteins.
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PMID:The helical content of zein, a water insoluble protein, in non-aqueous solvents. 112 75

Infrared absorption spectroscopy has been used to study the effect of organic solvents on the conformation of myoglobin, apomyoglobin, hemoglobin, lysozyme and ribonuclease. Beta structure can easily be induced by specific solvent effects. Films prepared from a 50% (v/v) mixture of alcohol, acetone, pyridine, tetrahydrofuran or dimethylsulfoxide/water mixtures show a high proportion of beta structure. The degree of induction of beta structure depends on the hydrocarbon content of the alcohol in the order methanol greater than ethanol greater than butanol. No beta structure was observed in films prepared from aqueous octanol solutions. Lyophilization tends to decrease secondary structure. The conformation of the proteins depends on the particular solvent system and the solvent composition. Solution studies of myoglobin in pure dimethylsulfoxide show that the conformation is a mixture of random and beta forms while in dimethylsulfoxide/2H2O mixtures the conformation is a mixture of alpha-helical and beta forms.
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PMID:Infrared spectroscopic studies of solvent-induced conformational changes in globular proteins. 114 18


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