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The primary structure of leucine iso leucine valine binding protein from escherichia coli


, : The primary structure of leucine iso leucine valine binding protein from escherichia coli. Bioorganicheskaya Khimiya 3(4): 564-568

The complete amino acid sequence of periplasmic protein from E. coli, selectively binding branched aliphatic amino acids such as leucine, isoleucine and valine (LIV-protein), was established. Exhaustive tryptic hydrolysis and splitting of the protein molecule into large fragments at Met and Arg residues and Asp-Pro bonds with subsequent determination of their structure by automatic degradation were employed. The LIV-protein molecule consists of 344 amino acid residues.

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Grinkevich, V.A.; Arzamazova, N.M.; Grinkevich-Kh, A.; Akimenko, Z.A.; Moroz, I.N.; Nazimov, I.V.; Aldanova, N.A., 1979: Primary structure of leucine iso leucine valine binding protein from escherichia coli 2. cyanogen bromide peptides. The splitting of carboxymethylated Leu, Ile, Val(LIV)-binding protein from E. coli by CNBr was performed. By gel-filtration, DEAE-chromatography and paper chromatography, 5 individual peptides out of 6 formed on cleavage were isolated. The arrange...

Grinkevich, V.A.; Arzamazova, N.M.; Potapenko, N.A.; Grinkevich-Kh, A.; Kravchenko, Z.B.; Feigina, M.Y. ; Aldanova, N.A., 1979: Primary structure of leucine iso leucine valine binding protein from escherichia coli 1. the peptides of exhaustive tryptic hydrolysis. Exhaustive tryptic digestion of carboxymethylated Leu, IIe, Val (LIV)-binding protein was performed. For the initial separation of hydrolysate, chromatography on Aminex AG 50W .times. 4 resin and subsequent purification of peptides by paper chroma...

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