Studies on the modification of Escherichia coli ribosomal protein L7/L12 by succinic anhydride.
Lysine modification by increasing quantities of succinic anhydride in the Escherichia coli ribosomal protein L7/L12 produces loss of its ability in reconstitution of elongation-factor-G-dependent GTP hydrolysis and polyphenylalanine synthesis activities, showing lower antigenicity and loss of antigenic determinants.
D000939:Epitopes / Q000276:immunology; D004926:Escherichia coli / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism; D005779:Immunodiffusion; D008239:Lysine; D010452:Peptide Biosynthesis; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors / Q000494:pharmacology; D010455:Peptides; D012269:Ribosomal Proteins / Q000378:metabolism*; D013386:Succinates / Q000494:pharmacology*; D013387:Succinic Anhydrides / Q000494:pharmacology*
D000939:Epitopes; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D010455:Peptides; D012269:Ribosomal Proteins; D013386:Succinates; D013387:Succinic Anhydrides; C012001:polyphenylalanine; C016700:ribosomal protein L7-L12; D006160:Guanosine Triphosphate; D008239:Lysine