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)

1. Alkaline ribonuclease (pH optimum 7.6) was isolated from rye (Secale cereale L) germ cytosol and partially purified; the preparation was devoid of other nucleolytic activities. 2. The enzyme is a typical endonuclease hydrolysing all phosphodiester bonds in RNA, yielding ultimately purine and pyrimidine nucleoside 2',3'-cyclic phosphates and the corresponding 3'-phosphates. Upon extensive digestion of synthetic polyribonucleotides, pyrimidine, but not purine, nucleoside 3'-phosphates are formed. The enzyme does not hydrolyse synthetic purine cyclic nucleotides. 3. The enzyme does not depolymerize double-stranded complexes of poly(A) and poly(U). 4. Susceptibility to photooxidation and inhibition by 2-hydroxy-5-nitrobenzyl bromide and N-bromosuccinimide implies the involvement of tryptophan residue in the active centre of the enzyme.
Acta Biochim Pol 1976
PMID:Alkaline ribonuclease from rye germ cytosol. 0 57

Deoxyribonucleolytic activity was found to be associated with cytoplasmic ribosomes and ribosomal subunits of rye germs. The activity has the pH optimum at 5.0. Treatment of ribosomes and 60S subunits with 0.5 M-ammonium chloride released a considerable part of deoxyribonucleolytic and ribonucleolytic activity; treatment of 40S subunits resulted in a complete release of deoxyribonucleolytic activity and partial release of ribonucleolytic activity. This suggests the presence in ribosomes of rye germs of two types of nucleolytic enzymes: an enzyme of the nuclease I type with deoxyribonuclease and ribonuclease activities, and typical ribonucleases hydrolysing RNA only.
Acta Biochim Pol 1979
PMID:The presence of deoxyribonucleolytic activity in cytoplasmic ribosomes of rye (Secale cereale L) germs. 4 88

The nucleotide sequence of tRNAPhe of yellow lupin seeds (Lupinus luteus) is deduced from the composition of pancreatic and T1 ribonuclease digestion products and compared with tRNAPhe of wheat germ. Major lupin tRNAPhe, unlike pea tRNAPhe, differs from wheat germ tRNAPhe in the first base pair of stem TpsiC ("e").
Acta Biochim Pol 1977
PMID:Nucleotide sequence of tRNAPhe from the seeds of lupin (Lupinus luteus). Comparison of the major species with wheat germ tRNAPhe. 26 39

The binding isotherms of native bovine serum albumin with cationic detergents, such as octyl, decyl, dodecyl and tetradecylpyridinium bromides were determined at pH 6.8 and 3.4 at 25 degrees C. The isotherms for dodecyl and tetradecylpyridinium bromides were also determined at 3 degrees C. The average number of detergent cations bound increased with increasing hydrocarbon chain length. At low detergent concentration the binding of all alkylpyridinium bromides was smaller at pH 3.4 than at pH 6.8. Dodecylpyridinium bromide was bound to native beta-lactoglobulin, aldolase, ovalbumin, haemoglobin, myoglobin, lysozyme, trypsin and ribonuclease at pH 6.8. No binding occurred to alpha-chymotrypsin and chymotrypsinogen. The free enthalpy change, --delta G degrees, calculated from intrinsic association constants K was determined.
Acta Biochim Pol 1979
PMID:Protein-cationic detergent interaction. Equilibrium dialysis study of the interaction of bovine serum albumin and other proteins with alkylpyridinium bromide. 49 43

Fourier transform infrared and laser Raman spectroscopies were used to study the effects of dodecylpyridinium bromide on the conformation of haemoglobin, myoglobin, bovine serum albumin, ribonuclease, ovalbumin, lysozyme, trypsin and beta-lactoglobulin in aqueous solution. Addition of the cationic detergent caused a decrease in alpha-helix conformation in highly helical proteins. At low detergent concentrations stabilization of beta-sheet conformation was observed.
Acta Biochim Pol 1979
PMID:Protein-cationic detergent interaction. Fourier transform infrared and laser Raman spectroscopic studies on the interaction between proteins and dodecylpyridinium bromide. 49 44

Highly purified tRNAPhe from barley embryos was completely digested with pancreatic ribonuclease and T1 ribonuclease. The digestion products were separated using DEAE-cellulose chromatography. The Y base-containing fragment of the anticodon region of tRNAPhe has the following nucleotide sequence: Cpm2(2)GppsipCpApGpApCmpUpGmpApApYpAppsipCpUpGp, i.e. the same as in the anticodon region of wheat germ and pea tRNAPhe.
Acta Biochim Pol 1978
PMID:Nucleotide sequence of the anticodon region of barley embryo phenylalanine transfer RNA. 66 78

Acid and alkaline ribonuclease (RNase) activities were measured in serum and urine using procedure based on assumption that all determined RNase activities, both at pH 6.5 and 7.8 represent values produced by overlapping of activities of acid leukocyte type RNase and alkaline pancreatic type RNase. The procedure requires simultaneous determining of RNase activity at pH 6.5 and 7.8 and further calculation of actual activities of acid and alkaline RNase activities using the elaborated experimental formula. Results of determining acid and alkaline RNases in human sera yielded on information on specific contribution of leukocyte type and pancreatic type RNases to increased RNase activity in such clinical conditions as terminal renal failure, myocardial infarction and chronic myelogenous leukemia. It was also found that there is in human urine a remarkably increased proportion of acid RNase activity if compared to this in serum.
Mater Med Pol
PMID:Determining of actual activities of acid and alkaline ribonuclease in human serum and urine. 184 95

An in vitro transcription system was developed from H411EC3 (H4) hepatoma cells, which mimics the in vivo up-regulation by glucocorticoid hormones on ribosomal RNA (rRNA) synthesis. Ribosomal DNA (rDNA) transcription in extracts derived from H4 cells grown in the presence of 100 nM triamcinolone acetonide was 4- to 5-fold greater than that in extracts derived from cells grown in the absence of glucocorticoid. This effect was not a general stimulation by the steroid, as RNA polymerase II transcription of the metallothionein-1 gene which lacked a glucocorticoid responsive element was unaffected. The increased transcription in hormone-treated extracts was also independent of differential ribonuclease activities or inhibitors as ascertained by the inclusion of ribonuclease inhibitor and mixing experiments, respectively. Chromatography of H4 cell extracts on heparin-sepharose followed by transcription complementation analysis, showed that the hormone-induced stimulatory activity eluted with the fraction (TFIA) which contains RNA polymerase I (Pol I). Immunoblot analysis with specific anti-Pol I antibody showed similar subunit profiles in the absence and presence of the hormone. The presence of a Pol I enhancer element in addition to the rDNA promoter did not further modify the glucocorticoid-induced transcription. These results indicate that the glucocorticoid-mediated effects could be observed in cell extracts which accurately initiate transcription of cloned rat rDNA. Moreover, the alterations of rDNA transcription by the hormone is effected by a factor which elutes with fraction TFIA.
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PMID:Glucocorticoid-induced stimulation of ribosomal gene transcription in rat hepatoma cells is mediated by modification of RNA polymerase I or an associated factor. 260 60

The patterns of limited hydrolysis of yeast tRNA(Phe) and tRNA(-YPhe) by double strand-specific ribonuclease V1 show some differences in cleavage of both the acceptor stem and the anticodon stem. These regions are considerably better substrates for RNase V1 in tRNA(-YPhe) than in tRNA(Phe). The results are interpreted in favour of conformational changes taking place in yeast tRNA(Phe) upon the Y-base1 removal.
Acta Biochim Pol 1989
PMID:The response of the double strand-specific nuclease V1 to Y-base removal in yeast tRNA(Phe). 269 3

The effect of an empirical solvation energy term on energy minimization of ribonuclease T1 was established using different sets of Atomic Solvation Parameters. The results are compared to minimization in vacuo and in a 10 A water shell. The best solvent model as judged from the comparison to the crystal structure was an empirical solvation potential derived from free energies of transfer of amino-acid side-chain analogues from vapour to water. The use of this model causes, however, energy and gradient oscillations, which make it inapplicable with standard protocols of molecular dynamics simulations. The empirical solvation model which was found by other authors (von Freyberg et al., 1993, J. Mol. Biol. 233, 275-292) to give good results in the NMR structure refinement led to distortions of the ribonuclease native structure. The model based on statistical analysis of crystal structures did not perform better than minimization in vacuo.
Acta Biochim Pol 1997
PMID:Energy minimization of globular proteins with solvent effects included. Comparison of empirical solvation energy terms and explicit water treatment. 951 64


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