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Ribonuclease sequence analysis

If polyribonucleotides are treated simultaneously with methoxylamine and bisulphite, cytidine residues are converted into 5,6-dihydro-7V4-methoxycytidine-6-sulphonate,154 and uridine into 5,6-dihydrouridine-6-sulphonate.155 Treatment with dilute ammonia regenerates the uridine residues, leaving the dihydrocytidine derivatives unaffected. When only the cytidine residues have been derivatized, pancreatic ribonuclease becomes uridyl ribonuclease, since it is unable to cleave the chain on the 3 -side of the modified cytidine.154 This allows the isolation of blocks of modified cytidine residues. T2 ribonuclease may also be used. Alternatively, a ribonuclease from Physarum polycephalum has been found to hydrolyse CpX links very slowly, allowing the isolation of cytidine blocks.156 If both uridine and cytidine residues are modified, T2 ribonuclease acts as puryl ribonuclease, allowing the isolation of cumulative blocks of pyrimidines.155 This ability to alter the specificity of nuclease cleavage is a useful tool in sequence analysis. [Pg.173]

Top-down sequence analysis of whole glycoprotein ions using CID and ion/ion proton transfer in a quadrupole ion trap MS [66], This approach eliminated gas-phase deglycosylation of N-linked oligosaccharide in ribonuclease B, and the glycosylation site was identified to be Asn-Leu-Thr at residues 34-36 [66],... [Pg.863]

This was first foimd by Sanger et al. (1955) in a peptide from insulin and was observed with other peptides by Hirs et al. (1956) and Smyth et al. (1962). The reaction appears to occur when acidic buffers or dilute acids are employed for isolation of peptides. Conversion of the cyclic pyrrolidone carboxyl residue to a glutamyl residue is obtained on mild hydrolysis in dilute acids or alkalies. The cyclization reaction leads to difficulties when sequence methods are used which proceed from the amino-terminal end of a peptide. In addition, this reaction can occur when an internal glutamine residue becomes amino-terminal in the course of stepwise sequence analysis under acidic conditions, as in the Edman methods. An incorrect sequence for a peptide from ribonuclease was deduced as the result of cyclization of amino-terminal glutamine and acidic destruction of serine and threonine in the same peptide (Smyth et al., 1962). [Pg.57]

In 1960, Hirs, Moore, Stein, and Anfinsen described the first primary structure of the enzyme ribonuclease (M.W. 13,700), which has a single peptide chain of 124 amino acid residues and four intrachain disulfide bonds. These investigators established many of the techniques still used in sequence analysis, such as the use of ion exchange resins for separation of peptides and amino acids. [Pg.35]

Once the amino acid sequence of the peptide is determined, this sequence is searched in the protein databank to determine whether a protein containing this sequence exists. On such a search of the protein databank for this sequence Phe glu arg gin his met asp ser, it is found that it belongs to bovine ribonuclease A. This completes the identification and sequence analysis of this protein. [Pg.94]

Besides ribonuclease from the pancreas, enzymes from a mold are known to spht specifically at certain purine bases (Egami). This is important for the sequence analysis of nucleic acids. [Pg.144]

Ribonuclease U2 is a novel enzyme found in the culture broth of Ustilago sphaerogena (7, 106). Ribonuclease U2 splits, practically specifically, the phosphodiester bonds of purine nucleotides in RNA with the intermediary formation of purine nucleoside 2, 3 -cyclic phosphates, indicating the specificity is complementary to that of pancreatic RNase A (106). Like RNase N, RNase U2 very slowly hydrolyzes the intermediate, nucleoside 2, 3 -cyclic phosphate, to 3 -nucleotides (80, 106). Thus, RNase U2 is a useful tool, not only for the analysis of nucleotide sequences of RNA (90, 92, 107, 108) but also for the synthesis of various oligonucleotides containing adenylyl or guanylyl residue (30) (T. Koike, T. Uchida, and F. Egami, unpublished). [Pg.234]

Perform phylogenetic analysis by parsimony approach of ribonucleases with amino acid sequences given in Exercise 2. [Pg.281]

Ijeucine aminopeptidase has been applied in many ways to particular problems in structural analysis of peptides and proteins. Sequences in the amino-terminal portion of a peptide can often be established by measurement of the order of appearance of amino acids that are released during hydrolysis. The procedure has been used with a variety of proteins and peptides, including ribonuclease (Hirs et al., 1960), hemoglobin (Konigsberg and Hill, 1962, 1963 Schroeder et al., 1963), cytochrome c (Margoliash, 1962 Matsubara and Smith, 1963), and lysozyme (Canfield, 1963). [Pg.88]

The development of the continuous-flow FAB interface by Caprioli et al. [8] was primarily directed at the analysis of peptides (Ch. 4.6). Continuous-flow FAB provided reduced suppression of hydrophilic peptides in peptide mixtures. It was widely applied in the field of peptide characterization and the analysis of proteolytic digests, e.g., in the analysis of a tryptic digest of bovine ribonuclease B before and after treatment with N-glycanase [9]. A single injection of 100 pmol provided ca. 70% sequence coverage. [Pg.443]

Modified bases in the RNA will stop or pause the reverse transcriptase 3 to the modified base. Breaks in the RNA induced by ribonucleases or chemicals will also terminate the polymerase. The electrophoretic analysis of the reverse transcript reveals the stops as bands on an autoradiograph. The position of the modification or scission can be determined by co-electrophoresis of a dideoxy sequence reaction, and the intensity of the band will reflect the reactivity of the base (Figs 4.7 and 4.10). [Pg.131]

C-Linked glycosylation was first identified on ribonuclease 2 and is characterized by a-mannose (Man) attached to the 2-position of the indole side chain of tryptophan residues (Figure 6(b)). This modification has subsequently been identified on several proteins such as MUC5AC and MUC5B/ thrombospondin, and even the Ebola virus soluble glycoprotein. Analysis of protein databases for the putative C-linked mannosyla-tion consensus sequence, TrpXaaXaaTrp, suggests that a variety of proteins may bear this modification. The main role of C-linked mannosylation on protein remains to be determined. [Pg.266]

The first RNA molecule to be sequenced was not a virus, but a tRNA. Two enzymes were required in these analyses (i) bovine pancreatic ribonuclease, which cleaved after pyrimidines (C or U), became a classic system for scientific studies after Armour Co., the hotdog Company, purified 1 kg of the enzyme and distributed it to scientists (source Wikipedia) and (ii) takadiastase ribonuclease Tl, which cleaved 3 to a guanosine (G). Each of these small fragments was further analyzed by partial digestion with snake venom diesterase from the 3 -ends. Once again, biochemistry and enzymology led to breakthroughs in chemical analysis. [Pg.732]

The order in which the tryptic peptides occur must then be determined by another technique, e.g. according to a scheme of overlapping cleavages with other proteases (pepsin, ch3onotrypsin, papain, and others). The first extensive sequence of amino acids was determined on insulin (Sanger 1954), which is a polypeptide consisting of 51 amino acids. The sequential Analysis of true proteins was still beset with serious obstacles. Finally in 1959, ribonuclease vith 124 amino acid... [Pg.43]

For each entry, a table summarizes information regarding (1) the X-ray diffraction data upon which the analysis is based, (2) the methods employed in structure analysis and refinement and their main results, and (3) some structural characteristics. In a separate table, the ribonuclease amino acid sequence is... [Pg.36]


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Ribonuclease sequence

Sequence analysis

Sequencing analysis

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