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)

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

1. RNAases varying in pH optimum, activation with pCMB, sensitivity towards temperature and acid treatment, as well as electrophoretic mobility were found in Rana esculenta liver extract. 2. Of the three activity peaks of alkaline ribonuclease separated on CM-cellulose with 2000-fold purification, RNAase of peak C is thermo- and acid-stable and exhibits specificity for pyrimidine bases, preferring poly(U) over poly(C). 3. Differences in the specific "inhibitory effect" of frog liver supernatant on the frog liver alkaline RNAase were observed.
Acta Biochim Pol 1979
PMID:Partial purification and some properties of a liver alkaline ribonuclease from the frog Rana esculenta. 4 Mar 72

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

1. Large-scale isolation of tRNA from barley embryos is described, involving: phenol extraction, RNA deproteinization with the chloroform-isoamyl alcohol mixture, batch sorption on DEAE-cellulose, NaCl gradient elution of tRNA from DEAE-cellulose, and deaminoacylation of tRNA in the presence of bentonite. The procedure yielded tRNA free of protein and RNase activity. 2. The amino acid acceptor activity of the crude barley tRNA, its melting profiles and chromatographic patterns on Sephadex G-100 and BD-cellulose were similar to those of tRNA from other sources.
Acta Biochim Pol 1976
PMID:Large-scale isolation of tRNA from barley embryos. 93 83

Spleen cells (SpC) from nonimmunized CFW mice were converted into antibody plaque-forming cells (PFC) by incubation with RNA extracted from livers and spleens of immunized mice (4 days after a single intravenous injection of 0.2 ml of 5% sheep red blood cells (SRBC). RNA was extracted by the phenol-detergent procedure only when sensitization determined by the technique of Jerne showed at least one PFC per 1,500 SpC. Immunogenic activity of RNA from lives of immunized mice was identical with that of RNA from spleens. Immunogenic RNA was inactivated by RNase but not by DNase or pronase, indicating that induction of antibody synthesis requires intact RNA. Newly synthesized antibodies were specific for the SRBC injected antigen; plaques did not occur when other RBC were used in place of SRBC for the in vitro test. The influence of antibiotics on this phenomenon is also discussed.
Ann Med Sect Pol Acad Sci 1975
PMID:Induction of antibody synthesis in vitro by immunogenic RNA. 119 43

Modification of the method for determining low amounts of RNA and DNA is proposed. It consists in nucleic acid staining in solution with EtBr (1 microgram/ml) followed by photography of 10 microliters drops on a UV-transparent plate under UV illumination. Densitometric measurements of the Polaroid negatives were used to construct standard concentration curves in the range of 1-16 micrograms/ml of DNA or RNA. This permitted to determine nucleic acid in amounts as little as 10 micrograms. The measurements were not influenced by the presence of proteins such as bovine serum albumin, DNase, RNase or proteinase K, thus the method proposed may be useful in determining the nucleic acid content of very small samples or of scarce biological material.
Acta Biochim Pol 1990
PMID:Quantitation of nanogram amounts of nucleic acids in the presence of proteins by the ethidium bromide staining technique. 170 86


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