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)

Evidence that 32 S nRNA contains 5.8 S rRNA was provided by studies on specific oligonucleotide sequences of these RNA species. Purified 32P-labeled 5.8 and 28 S rRNA and 32 S RNA were digested with T-1 ribonuclease, and the products were fractionated according to chain length by chromatography on DEAE-Sephadex A-25 at neutral pH. The oligonucleotides in Peak 8 were treated with alkaline phosphatase and the products were separated by two-dimensional electrophoresis on cellulose acetate at pH 3.5 and DEAE-paper in 7% formic acid. Seven unique oligonucleotide markers for 5.8 S rRNA including the methylated octanucleotide A-A-U-U-Gm-G-A-Gp were present in 32 S RNA but were not found in 28 S rRNA, indicating that 5.8 S rRNA is directly derived from the 32 S nucleolar precursor. These studies confirm a maturation pathway for rRNA species in which 32 S nucleolar RNA is a precursor of 5.8 S rRNA as well as 28 S rRNA.
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PMID:Maturation pathway for Novikoff ascites hepatoma 5.8 S ribosomal ribonucleic acid. Evidence for its presence in 32 S nuclear ribonucleic acid. 16 43

The sequences of amino acid residues 15-23 of red deer (Cervus elaphus) and roe deer (Capreolus capreolus) pancreatic ribonuclease and the identity of residue 99 in roe deer ribonuclease are corrected. Earlier results are explained by the cleavage of an Asp-Pro bond in both enzymes during the treatment with CNBr in 70% formic acid and by wrong interpretations of amino acid analyses. Proline residues, which occur at a number of positions in several mammalian ribonucleases, can be accommodated in a model of bovine ribonuclease S without disrupting the conformation of the main chain.
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PMID:Reinvestigation of the primary structures of red deer and roe deer pancreatic ribonuclease and proline sites in mammalian ribonucleases. 83 89

Ribonucleoprotein particles were isolated from unfertilized eggs and gastrula stages of Xenopus laevis. The particles from both stages induce in gastrula ectoderm the formation of large foreheads (neural-archencephalic-inducing activity), whereas ribosomal subunits have no inducing activity. The inducing activity of particles from both stages is largely abolished after treatment with proteolytic enzymes and to some extent with ribonuclease. The protein moiety of gastrula ribonucleoprotein particles was extracted with phenol and the protein reduced with 2-mercaptoethanol. The protein induces foreheads, but at a lower rate than the intact particles. The protein was fractionated by high-performance liquid size-exclusion chromatography on a derivatized silica gel with 75% formic acid as eluent. The fraction which includes proteins from 10 000 to 16 000 Da has the highest neural-archencephalic-inducing activity.
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PMID:Ribonucleoprotein particles from Xenopus eggs and embryos. Neural-archencephalic-inducing activity of the protein moiety. 637 Jun 94

Bovine ribonuclease B (RNAse B) and asialofetuin (FETUA) were subjected to in-capillary tryptic digest (Pohlentz et al. Proteomics. 2005, 5, 1758-1763) and the obtained glycopeptides were analyzed, respectively, by nanoelectrospray ionization mass spectrometry and collision-induced dissociation (CID) during the ongoing digest. For RNAse, B glycans of the high-mannose type (Man(4) to Man(9)) attached to either a tetra- or a hexapeptide containing the sole N-glycosylation site of the protein were detected. Glycopeptides derived from all three N-glycosylation sites of FETUA were observed, and the corresponding CID spectra proved the respective glycans to be oligosaccharides of the triantennary complex type. Moreover, an O-glycopeptide carrying Gal-GalNAc at T(280) could be unambiguously identified. An in-solution tryptic/chymotryptic digest of human transferrin (TRFE) was analyzed directly for glycopeptides subsequent to the addition of methanol and formic acid. Disialylated diantennary glycans were observed in glycopeptides of both N-glycosylation sites of TRFE. These results demonstrate the feasibility of direct structure determination of glycopeptides in proteolytic mixtures without any further refurbishment.
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PMID:Structure elucidation of glycoproteins by direct nanoESI MS and MS/MS analysis of proteolytic glycopeptides. 1796 May 75

One of the most frequently used high-resolution glycan analysis methods in the biopharmaceutical and biomedical fields is capillary electrophoresis with laser-induced fluorescence (CE-LIF) detection. Glycans are usually labeled by reductive amination with a charged fluorophore containing a primary amine, which reacts with the aldehyde group at the reducing end of the glycan structures. In this reaction, first a Schiff base is formed that is reduced to form a stable conjugate by a hydrogenation reagent, such as sodium cyanoborohydride. In large scale biopharmaceutical applications, such as clone selection for glycoprotein therapeutics, hundreds of reactions are accomplished simultaneously, so the HCN generated in the process poses a safety concern. To alleviate this issue, here we propose catalytic hydrogen transfer from formic acid catalyzed by water-soluble iridium(III)- and ruthenium(II)-phosphine complexes as a novel alternative to hydrogenation. The easily synthesized water-soluble iridium(III) and the ruthenium(II) hydrido complexes showed high catalytic activity in carbohydrate labeling. This procedure is environmentally friendly and reduces the health risks for the industry. Using carbohydrate standards, oligosaccharides released from glycoproteins with highly sialylated (fetuin), high mannose (ribonuclease B) and mixed sialo and neutral (human plasma) N-glycans, we demonstrated similar labeling efficiencies for iridium(III) dihydride to that of the conventionally used sodium cyanoborohydride based reaction. The derivatization reaction time was less than 20min with no bias towards the above mentioned specific glycan structures.
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PMID:A novel carbohydrate labeling method utilizing transfer hydrogenation-mediated reductive amination. 2853 51