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The primary structure of leucine iso leucine valine binding protein from escherichia coli 3. the peptides of restricted tryptic and limited acidic hydrolysis determination of a di sulfide bridge in the protein molecule


, : The primary structure of leucine iso leucine valine binding protein from escherichia coli 3. the peptides of restricted tryptic and limited acidic hydrolysis determination of a di sulfide bridge in the protein molecule. Bioorganicheskaya Khimiya 6(1): 31-45

Tryptic hydrolysis of carboxymethylated, maleylated Leu, Ile, Val (LIV)-binding protein from E. coli was performed. By gel-filtration, DEAE-chromatography and paper chromatography, 8 individual peptides were isolated. The complete structures of 6 peptides and partial amino acid sequences of 2 peptides were determined. Acidic hydrolysis at Asp-Pro bonds reslted in 4 fragments, which were resolved by gel-filtration and DEAE-chromatography. The structural analysis of the obtained peptides allowed to complete the reconstruction of the polypeptide chain of the protein. The presence of a disulfide bridge in the LIV-protein was established by 2 different methods.

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