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)

The diagnostical relevance of the low-molecular proteins ribonuclease, beta 2-microglobulin and lysozyme in serum and urine to detect a reduced glomerular filtration rate was examined in 52 patients with chronic renal diseases. The radioisotope clearance using 99mTc-DTPA was the base reference; the reference values of the low-molecular proteins were estimated in a control group. Ribonuclease was increased above the upper borderline value, if the glomerular filtration rate was lower than 1.24 ml s-1. Creatinine, beta 2-microglobulin and lysozyme remain yet in part in the normal range. The estimation of the ribonuclease in serum is suitable to detect an impaired glomerular filtration rate if the creatinine value is still not increased. Thereby, the diagnostics in renal diseases may be improved in the creatinine-blind area.
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PMID:[The low molecular weight proteins ribonuclease, beta 2 microglobulin and lysozyme in the serum and urine of patients with chronic kidney diseases]. 307 Oct 37

Using automated Edman degradation of two nonfractionated peptide mixtures of tryptic and staphylococcal protease digests of the protein, the complete amino acid sequence of the guanyl-specific ribonuclease Sa from Streptomyces aureofaciens was established. Ribonuclease Sa contains 96 amino acid residues (Mr 10,566). A 50% sequence homology of ribonuclease Sa to the guanyl-specific ribonuclease St from S. erythreus was found.
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PMID:Amino acid sequence determination of guanyl-specific ribonuclease Sa from Streptomyces aureofaciens. 309 82

Ribonuclease T1 (RNase T1, EC 3.1.27.3) is a guanosine-specific ribonuclease that cleaves the 3',5'-phosphodiester linkage of single-stranded RNA. It is assumed that the reaction is generated by concerted acid-base catalysis between residues Glu-58 and His-92 or His-40. From the results of chemical modification and NMR studies, it appeared that the residue Glu-58 was indispensable for nucleolytic activity. However, we have recently demonstrated that Glu-58 is an important but not an essential residue for catalytic activity, using the methods of genetic engineering to change Glu-58 to Gln-58 etc [Nishikawa, S., Morioka, H., Fuchimura, K., Tanaka, T., Uesugi, S., Ohtsuka, E., & Ikehara, M. (1986) Biochem. Biophys. Res. Commun. 138, 789-794]. In the present paper, we report that mutants of RNase T1 with residue Ala-40 or Ala-92 have almost no activity, while mutants that contain Ala-58 retain considerable activity. These results show that the two histidine residues, His-40 and His-92, but not Glu-58, are indispensable for the catalytic activity of the enzyme. We propose a revised reaction mechanism in which two histidine residues play a major role, as they do in the case of RNase A.
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PMID:Two histidine residues are essential for ribonuclease T1 activity as is the case for ribonuclease A. 312 7

Ribonuclease Ms from Aspergillus saitoi is a small acidic protein (11,714 Da) containing 106 amino acids of known sequence. Unlike other enzymes belonging to the RNase T1 family this ribonuclease is base-unspecific. Using interactive computer graphics and energy minimisation we predicted the structure of RNase Ms on the basis of sequence homology to RNase T1 of known structure. In this report the predicted structure of this protein is presented and characterised.
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PMID:The tertiary structure of Aspergillus saitoi minor ribonuclease (Ms) predicted from the structure of RNase T1. 314 94

The organization of select proteins within ribonucleoprotein particles containing heterogeneous nuclear and uridine-rich small nuclear RNAs (hnRNP and UsnRNP respectively) was examined by chemical cross-linking and ribonuclease digestion using diagonal two dimensional PAGE and immunoblotting detection systems. Monoclonal antibodies specific for A2, C1 and C2 hnRNP proteins, detected these proteins at gel coordinates which suggested homotypic dimers and trimers of A2 and homotypic trimers, hexamers and larger multimers of C1 and C2. Ribonuclease digestion did not alter the cross-linking properties of hnRNP C1 and C2 proteins but did result in loss of A2 homotypic dimers and trimers. Blots simultaneously reacted with hnRNP specific monoclonal antibodies and autoimmune patient serum (RNP/Sm), or monoclonal antibodies reactive with the U1 snRNP specific 63 kDa protein and/or the UsnRNP common proteins B', B and D revealed no complexes which would indicate interactions between hnRNPs and UsnRNPs. The U1 UsnRNP specific 63 kDa protein appeared not to be cross-linked to UsnRNP common B', B and D proteins. The data also suggested that UsnRNP common protein D was cross-linkable to UsnRNP common proteins D', E and G but not to B' and B. The cross-linking properties of D were unaffected by ribonuclease digestion. In contrast, ribonuclease digestion resulted in an inability to cross-link select complexes containing either B' and B, or p63. The data suggest that both hnRNPs and UsnRNPs are comprised of RNA-dependent and RNA-independent protein-protein interactions.
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PMID:Reversible chemical cross-linking and ribonuclease digestion analysis of the organization of proteins in ribonucleoprotein particles. 323 Dec 14

Ribonuclease from bovine seminal plasma (RNase BS) interacts with skeletal muscle actin in the following way: it binds to actin with an apparent binding constant of 9.2 X 10(4) M-1 in 0.1 M KCl, induces the polymerization of actin below the critical concentration in depolymerization buffer, accelerates the salt-induced polymerization of actin even at a molar ratio of RNase to actin lower than 1/100, and bundles F-actin filaments. In the bundles the molar ratio of RNase to actin is about 0.66. Actin inhibits the enzymatic activity of RNase BS. RNase A from bovine pancreas, which is structurally almost identical to the subunits of RNase BS as well as a monomeric form of RNase BS, do not cross-link actin filaments and have a much smaller effect on the polymerization of actin. We conclude that the dimeric structure of the RNase BS, which consists of two identical subunits cross-linked by interchain disulfide bridges, is probably responsible for the bundling activity and the accelerating effect on the polymerization of actin.
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PMID:On the interaction of bovine seminal RNase with actin in vitro. 329 98

The diagnostic value of the low-molecular mass proteins ribonuclease, beta 2-microglobulin, and lysozyme in serum for the detection of reduced glomerular filtration rates was evaluated. The values of these proteins and of serum creatinine investigated in 52 patients suffering from chronic renal diseases were plotted against 99m-Tc-diethylenetriaminopentaacetate clearance as an indicator of glomerular filtration rate. Log-transformed data showed a good fit of linearity. Considering the 95% confidence limits of the regression equations, ribonuclease increased above the normal range when the glomerular filtration rate was lower than 1.24 ml/s whereas the other analytes partly remained within their normal limits. Out of those 18 patients with glomerular filtration rates lower than 1.24 ml/s, all patients showed elevated ribonuclease levels. beta 2-Microglobulin, creatinine, and lysozyme were increased in 17, 14, and 12 cases, respectively. Ribonuclease and beta 2-microglobulin showed similar results when other diagnostic criteria (specificity, efficiency and predictive values) were taken into account. We recommend ribonuclease determination in serum for the detection of reduced glomerular filtration rate in the normal range of creatinine. The test is diagnostically powerful, cheap and easy to perform.
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PMID:Diagnostic value of low-molecular mass proteins in serum for the detection of reduced glomerular filtration rate. 332 Feb 63

1. The properties of a soluble ribonuclease from Aedes aegypti larvae have been compared with ribonuclease activity in adult female tissue. 2. In larval extracts ribonuclease activity was maximal at 40-45 degrees C whereas activity in tissue from adult females was highest at 50 degrees C. 3. Ribonuclease activity that was recovered in a 20-60% ammonium sulfate precipitate was further purified by batch elution from DEAE-Sephacel and from carboxymethylcellulose. 4. Ribonuclease activity in the partially purified fraction was sensitive to EDTA, stimulated by magnesium, had a pH optimum at 9.0 and a Mr of 45,000. 5. Agarose gels containing yeast RNA substrate were used to monitor partial purification of the larval ribonuclease.
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PMID:Properties of a ribonuclease from Aedes aegypti larvae. 342 5

Techniques of in vitro receptor autoradiography were used to visualize binding of 125I-insulin on slices of frozen rat brain. Slide-mounted sections of frozen rat brain were incubated in 0.05 nM porcine 125I-monoiodoinsulin, alone or mixed with 1 microM unlabeled porcine insulin, ribonuclease, or glucagon, for 2 h at 22 degrees C. The labeled brain slices were apposed to LKB Ultrofilm to generate autoradiograms. The method permitted equal access of labeled insulin to both sides of the blood-brain barrier and localization of insulin binding sites in small anatomic regions. Quantitative estimates of specific iodoinsulin binding were made by computer digital image densitometry of the autoradiographic film images. High concentrations of specific binding sites for iodoinsulin were present in the choroid plexus of the lateral (26.9 +/- 2.0 X 10(-3) fmol/mm2), fourth (18.3 +/- 3.0 X 10(-3) fmol/mm2), and third (13.2 +/- 1.5 X 10(-3) fmol/mm2) ventricles (insulin binding is expressed per unit area of autoradiographic image). Binding to the third ventricular choroid plexus was similar to the concentrations observed for liver slices and the external plexiform layer of the olfactory bulb. Specific binding of iodoinsulin in the cingulate cortex and other surrounding regions was less than in choroid plexus. Ribonuclease or glucagon had no measurable effect on binding when mixed with labeled insulin. The results support the hypothesis that the choroid plexus has a high density of receptors for insulin, and suggests that the choroid plexus may be a target of CSF insulin action and/or a site of insulin transport into the CSF.
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PMID:Quantitative autoradiographic evidence for insulin receptors in the choroid plexus of the rat brain. 351 Sep 31

Ribonuclease UL purified from pooled human urine contains approximately 20.7% of neutral sugar and 7.8% of aminosugar. All sugars were quantitatively released as oligosaccharides on hydrazinolysis. The oligosaccharides were converted to tritium-labeled oligosaccharides on reduction with NaB3H4. The radioactive oligosaccharide fraction was separated into a neutral and an acidic fraction on paper electrophoresis. All oligosaccharides in the acidic fraction could be converted to neutral oligosaccharides with the release of one sialic acid residue by sialidase digestion. Both fractions were shown to be mixtures of more than fourteen oligosaccharides by gel permeation chromatography. Structural studies on these oligosaccharides involving sequential exoglycosidase digestion in combination with methylation analysis revealed that ribonuclease UL contains sialylated and non-sialylated mono, bi-, tri-, and tetraantennary complex type sugar chains with N-acetyllactosamine outer chains, and tri- and tetraantennary complex type sugar chains with various numbers of Gal beta 1----4GlcNAc beta 1----3Gal beta 1----4GlcNAc beta 1----outer chains. An important finding was that all sialic acid residues in the acidic oligosaccharides only occur as the Sia alpha 2----6Gal beta 1----4GlcNAc beta 1----2Man alpha 1----3 group. Both fucosylated and non-fucosylated trimannosyl cores were found among the asparagine-linked sugar chains of ribonuclease UL.
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PMID:The carbohydrate moieties of human urinary ribonuclease UL. 357 Dec 8


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