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:3.1.26.9 (ribonuclease)
6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Polyribosomes were isolated from the intestinal mucosa of fasted and fat-fed rats in the presence of ribonuclease inhibitors. Polyribosomes from fat-fed rats were larger and more efficient in incorporating radioactive aminoacids into proteins than those from fasted rats. Total RNA prepared by guanidine-HCl extraction, from the intestine of fasting and fat-fed rats were translated in vitro in a mRNA-dependent rabbit reticulocyte lysate system in the presence of 35S-methionine. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and autoradiography of the synthesized peptides showed a relative increase in the radioactivity of some peptides of RNA from fat-fed animals and particularly a two fold increase in preapo-AIV indicating that the intestinal apo-AIV synthesis is under transcriptional regulation by the metabolic processes involved in fat transport, that is, triglyceride-rich lipoprotein production.
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PMID:Isolation and characterization of rat intestinal polyribosomes and RNA during absorption of fat. Increased translation in vitro of apo-AIV. 257 92

Two developments have enabled major advancements in the use of capillary gas chromatography (GC), the result being its much more widespread use in investigations on a broad range of chemical and biological problems. The 2 technological developments were the introduction of fused silica capillary columns and the development of immobilized stationary phases for capillary GC columns. Because fused silica columns with immobilized stationary phases of varying polarities are offered by numerous vendors of chromatographic equipment, they have become widely used for many analytical tasks. We conducted a study to compare the effectiveness of commercially available fused silica capillary columns with the classical ion-exchange method in the separation and quantitation of amino acids. We selected the N-trifluoroacetyl (TFA) n-butyl and the N-heptafluorobutyryl (HFB) isobutyl ester derivatives for this study because of the extensive research and application of these derivatives during the past 20 years. The amino acid content of hydrolysates of 5 materials was measured: ribonuclease, beta-lactoglobulin, lysozyme, soybean meal, and a commercial poultry feed. Single 6N HCl hydrolysates of each material were prepared to minimize sample preparation differences, and 3 independent analyses of each hydrolysate were made by each of 3 techniques: the N-TFA n-butyl and N-HFB isobutyl ester methods using capillary gas chromatography and the ion-exchange chromatographic method using a Beckman 121 M amino acid analyzer. Our results clearly demonstrate that capillary GC analysis of amino acids using fused silica bonded-phase columns provides data with good precision and in general excellent agreement with ion-exchange analyses.
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PMID:Amino acid analysis by capillary gas chromatography. 357 Nov 20

An optimized assay is described for the catalytic activity determination of serum ribonuclease, using polycytidylic acid as substrate and measuring the released acid-soluble ultra-violet absorbing products. Recommended final reaction concentrations are 0.3 mmol/l polycytidylic acid, 200 mmol/l imidazole/HCl buffer, pH 7.0, and 50 mmol/l NaCl. Optimal concentrations for the precipitation procedure, guaranteeing sufficient precipitation and minimal decomposition of unreacted substrate, are 160 mmol/l perchloric acid and 4 mmol/l lanthanum nitrate. Coefficients of variation for the method (within series and between days) ranged from 2.2 to 7.9%. No sex-related differences of catalytic activity were observed. In 63 blood donors with normal values of serum creatinine, the upper limit of the reference intervals (99th percentile) was 33.7 kU/l.
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PMID:An optimized micromethod for determining the catalytic activity of serum ribonuclease. 370 Dec 75

The vitamin B(12)-binding property of Lactobacillus leichmannii ATCC 7830 has been studied. The organism could bind 0.52 mug of B(12) per mg of cells. With regard to the cellular site for B(12) accumulation, three-quarters of the B(12) bound to the cell was found in the crude cell wall fraction, and the remaining one-quarter was found in the particulate (ribosome) fraction. After receiving enzymatic treatments with ribonuclease, lipase, and trypsin, the wall fraction retained three-fifths of the initial B(12). The possibility of cross-contamination of the wall and particulate fractions was excluded by measuring the contents of ribonucleic acid and hexosamines in each fraction. The B(12)-binding activity of the wall was destroyed by pretreatment of the wall with pepsin, Pronase, or trypsin. However, once bound to the wall, the B(12) was not released by the same treatments. These facts suggest that B(12) is bound to a polypeptide in the wall on which these enzymes act and that, once bound, B(12) somehow inhibits the enzymatic actions as described earlier with L. delbrueckii no. 1. A B(12)-polypeptide complex was isolated by treatment with 0.2 n HCl from walls to which B(12) had been bound. The complex was then purified. The complex moves as a single band on polyacrylamide gel electrophoresis. Its molecular weight was estimated around 21,500 with microheterogeneity on a Sephadex G-75 column. The mode of B(12) binding was found to be similar to that of L. delbrueckii.
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PMID:Further studies on the binding of vitamin B 12 to the cell wall of a B 12 -requiring Lactobacillus. 455 Jun 59

The biological activity of Odontomyces viscosus, which has been reported to cause periodontal disease in hamsters, was examined. The microorganism was cultured anaerobically in Brain Heart Infusion broth, and the cells were harvested. The washed cells were injected intradermally into the abdomen of rabbits. After 72 hr, a well-defined, firm, raised nodule (about 1.0 by 1.5 cm) with an erythematous border was seen at the injection site. Suspensions of cell wall and cytoplasmic material were injected intradermally, and the lesions appeared only at the site of cell wall injection. The cell walls, which were then treated with trypsin, pepsin, and ribonuclease, again produced the characteristic lesion. These nodular dermal lesions persisted for a minimal time of 10 days. The enzymatically treated cell walls were then hydrolyzed with 1 n HCl, and such hydrolysis up to 1 hr failed to alter the toxic activity of the cell walls. Similar dermal nodular lesions were obtained by injection of enzymatically treated cell walls of strains of Staphylococcus aureus, Streptococcus groups B, C, E, F, K, Lactobacillus casei, and Actinomyces israelii. Treatment with hot and cold trichloroacetic acid solutions and proteolytic enzymes, or with formamide, yielded insoluble fractions which produced the characteristic nodular lesions. The size of the lesion resulting from injection of these fractions was proportional to the amount of the injected material. The active fraction, which does not appear susceptible to hydrolysis by lysozyme, is thought to be cell wall mucopeptide. Histological studies showed skin abscesses due to the toxic reaction; however, in addition to the acute inflammatory reaction, there was local eosinophilia.
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PMID:Toxic properties of the cell wall of gram-positive bacteria. 533

Polyspermine-ribonuclease (Mr approximately 17 000) and the enzyme transcriptase from Rauscher-leukaemia virus (Mr approximately 70 000) form a complex Mr approx. 160 000) such that the molar ratio of polyspermine-ribonuclease to reverse transcriptase is 5:1. The most favourable condition for complex-formation is in a solution consisting of 0.01 M-Tris/HCl buffer, pH 7.5, 0.25 M-KCl and 1 mM-Mn2+ at 37 degrees C. The association of the two enzymes retains full RNAase activity, but reverse-transcriptase activity is completely inhibited when ribonuclease-sensitive polymers such as (dG)12 x (rC)n or viral 70S RNA are used as primer templates.
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PMID:Complexing reverse transcriptase with polyspermine-ribonuclease. 616 6

The reaction of ribonuclease (RNase) with N-[[(iodoacetyl)amino]ethyl]-5-naphthylamine-1-sulfonic acid (1,5-IAENS) yields a derivative in which one fluorescent group is covalently attached to the protein. Several arguments suggest that the chemical modification has occurred at the enzyme active site: (i) 1,5-IAENS should have the same specificity as iodoacetamide, i.e., carboxymethylate one histidine of the active site; (ii) the derivatized protein is enzymatically inactive; (iii) in the native state of the protein, the fluorescent group is (almost) completely protected from the aqueous solvent; (iv) this group has no motions other than those of the protein. The fluorescence properties of the derivatized RNase change markedly upon unfolding induced by guanidine hydrochloride (Gdn . HCl), as seen from fluorescence intensity, maximum emission wavelength, and polarization measurements. Upon Gdn . HCl-induced unfolding, the fluorescent group is transferred from a nonpolar to a highly polar environment. Dynamic fluorescence measurements show also that unfolding results in a markedly increased mobility of the fluorescent label with respect to its proteic environment. These results are compared to those of Young & Potts (1963) [Young, D. M., & Potts, J. T. (1963) J. Biol. Chem. 238, 1995--2002], who studied the fluorescence properties of a surface-labeled derivative of RNase.
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PMID:Fluorescent probe of ribonuclease A conformation. 627 83

The isolation and characterization of the initial intermediates formed during the irreversible acid denaturation of enzyme Ribonuclease A are described. The products obtained when RNase A is maintained in 0.5 M HCl at 30 degrees for periods up to 20 h have been analyzed by ion-exchange chromatography on Amberlite XE-64. Four distinct components were found to elute earlier to RNase A; these have been designated RNase Aa2, Aa1c, Aa1b, and Aa1a in order of their elution. With the exception of RNase Aa2, the other components are nearly as active as RNase A. Polyacrylamide gel electrophoresis at near-neutral pH indicated that RNase Aa1a, Aa1b, and Aa1c are monodeamidated derivatives of RNase A; RNase Aa1c contains, in addition, a small amount of a dideamidated component. RNase Aa2, which has 75% enzymic activity as compared to RNase A, consists of dideamidated and higher deamidated derivatives of RNase A. Except for differences in the proteolytic susceptibilities at an elevated temperature or acidic pH, the monodeamidated derivatives were found to have very nearly the same enzymic activity and the compact folded structure as the native enzyme. Fingerprint analyses of the tryptic peptides of monodeamidated derivatives have shown that the deamidations are restricted to an amide cluster in the region 67-74 of the polypeptide chain. The initial acid-catalyzed deamidation occurs in and around the 65-72 disulfide loop giving rise to at least three distinct monodeamidated derivatives of RNase A without an appreciable change in the catalytic activity and conformation of the ribonuclease molecule. Significance of this specific deamidation occurring in highly acidic conditions, and the biological implications of the physiological deamidation reactions of proteins are discussed.
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PMID:Isolation and characterization of monodeamidated derivatives of bovine pancreatic ribonuclease A. 642 73

We have developed a rapid and sensitive method for detecting ribonuclease (RNAase). The method makes use of a RNA-Pyronine Y complex which has a different absorption spectrum from that of Pyronine Y alone. When the RNA is hydrolyzed by RNAase, the spectrum of the complex changes to that of unbound Pyronine Y. The resultant decrease in absorbance at 572 nm is linear for final RNAase concentrations ranging from 2 to 45 ng/ml. Optimal assay conditions were 11.5 micrograms/ml Pyronine Y, 0.56 mg/ml RNA, 80 mumol/ml Tris-HCl buffer, pH 7.8, and 2-45 ng/ml RNAase. The effect of complex concentration, pH, molarity and temperature upon the rate of the reaction were determined. The assay is applicable to crude cell-free extracts.
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PMID:A simple spectrophotometric method for the measurement of ribonuclease activity in biological fluids. 666 3

The slow refolding of guanidine-HCl-denatured ribonuclease-A was studied by volume change and by kinetic CD at 222 and 276 nm. Dilatometric measurements revealed that on refolding there is a fast volume change of +232 mL/mol of protein. This is followed by a very slow nonexponential change that takes about 25 min to reach equilibrium. By adding varying amounts of (NH4)2SO4, the slow volume change curve was resolved into 2 concurrent reactions. The faster of the 2 slow events entails a negative volume change of -64 mL/mol of protein and appears to arise from proline isomerization. The slower process, attended by a positive change of +53 mL/mol of protein, has properties consistent with the "XY" reaction of Lin and Brands (1983, Biochemistry 22:563-573). This reaction is so named because the conformational nature of neither its initial (Y) nor its final state (X) is known; the transition is characterized solely by its absorbance and fluorescence kinetics. These are the first direct physical measures attributable to the "XY" process. The early formation of a compact structure in the event responsible for the rapid +232-mL/mol volume change, however, is consistent with the sequential model of folding (Cook KH, Schmid FX, Baldwin RL, 1979, Proc Natl Acad Sci USA 76:6157-6161; Kim PS, Baldwin RL, 1980, Biochemistry 19:6124-6129). The usefulness of volume change measurements as a method of detecting structural rearrangements was confirmed by finding agreement between time constants obtained from parallel volume change and kinetic CD experiments. The measured volume changes arise from both changes in hydration and changes in the packing of atoms in the interior of the protein.
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PMID:Slow-folding kinetics of ribonuclease-A by volume change and circular dichroism: evidence for two independent reactions. 800 82


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