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- W1569501791 abstract "Abstract Two tryptic hydrolysates of bovine liver glutamate dehydrogenase which had been maleylated prior to digestion were investigated. In one of these the carboxymethylated protein was used, in the other the protein had been oxidized with performic acid. These soluble derivatives were rapidly hydrolyzed by trypsin and after approximately 5 min, no additional hydrolysis was observed. From these two digests peptides accounting for 474 of the known 506 residues of the polypeptide chain were isolated. These peptides ranged in size from 2 to 73 residues. As expected, some of these peptides contained arginine as the only basic residue, indicating that these peptides are preceded by arginyl residues. Other peptides contained from 1 to 7 lysyl residues with a single arginyl residue, which was COOH-terminal in the peptide. Such peptides supplied overlaps for the component lysyl tryptic peptides. Many peptides were isolated which contained from 2 to 4 arginyl residues as well as several lysyl residues, thus providing additional overlaps at arginyl residues. Several segments of the protein were obtained which had not been found in fragments produced by other methods of scission. In all, the peptides obtained in this investigation established or confirmed 31 of the 33 overlapping sequences involving lysyl residues and at 9 arginyl residues as well. Some evidence is presented to explain the observations of limited action of trypsin at many arginyl residues. This appears to be due to the presence, at or near the potentially susceptible bond, of either acidic residues in the sequence itself or to hydroxyl groups which had become partially or completely maleylated. This is consonant with out observations that many peptides of identical composition manifested different electrophoretic mobilities or appeared in different fractions eluted from ion exchange columns." @default.
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- W1569501791 date "1971-04-01" @default.
- W1569501791 modified "2023-09-30" @default.
- W1569501791 title "Sequence of Bovine Liver Glutamate Dehydrogenase" @default.
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- W1569501791 doi "https://doi.org/10.1016/s0021-9258(18)62303-8" @default.
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