Publications by authors named "I N Telezhinskaia"

The main scientific sequence databases of interest for researchers working in the field of bioorganic chemistry are reviewed. Information is given concerning possibilities for rapid access and efficient search for needed information, postal and e-mail addresses, and literature sources in which these databases are comprehensively described.

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A major immunodominant envelope protein p35 of vaccina virus was purified by means of extraction from virions with detergent NP-40. The protein was cleaved with CNBr, four homogenous peptides were isolated and their N-terminal amino acid sequences were determined. Computer search in a protein sequences data bank revealed that the immunodominant protein p35 of vaccinia virus is encoded by H3 gene in HindIII-H fragment of vaccinia virus genome.

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Analysis of the Chloroflexus aurantiacus reaction centre (RC) using both protein and recombinant DNA techniques resulted in determination of its polypeptide composition and the primary structures of its two subunits. A model of the polypeptide chains' folding in the membrane is suggested based on: i) homology between L- and M-subunits of Chloroflexus aurantiacus RC and their counterparts in purple bacteria; ii) comparison of their hydropathy plots, and iii) data on the tertiary structures of purple bacteria RCs. The role of a number of functionally important amino acid residues in the RC electron transport activity is discussed.

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The spermatic protein of chromatin I2 of squid Illex argentinus was separated by HPLC into two components I2-1 and I2-2. Amino acid sequences of the major portion of protein I2-1 (52 residues) and the N-terminal sequence of protein I2-2 (21 residues) were determined. Arginines in protein I2-1 are arranged in clusters typical of protamines; the first cluster is in the N-terminus, the longest heterogeneous basic cluster is in the central part of the protein chain, the C-terminal part of the molecule contains two clusters of three hydroxyamino acids each.

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Method of isolation of the bovine pancreas tryptophanyl-tRNA synthetase is improved and a protein with greater than or equal to 99% purity, according to PAGE-SDS, is obtained. The pure enzyme is digested with clostripain and the hydrolysate is separated by FPLC anion-exchange chromatography followed by reversed phase HPLC. Amino acid sequences of 6 individual peptides, including C-terminal one, were determined by the automated Edman degradation.

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