Open AccessBinding of N -Substituted Erythromycylamines to Ribosomes
Author(s) -
Robert Vince,
David S. Weiss,
Sidney Pestka
Publication year - 1976
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.9.1.131
Subject(s) - ribosome , peptidyl transferase , binding site , fluorescein isothiocyanate , chemistry , escherichia coli , fluorescein , dissociation constant , fluorescence , isothiocyanate , stereochemistry , biochemistry , rna , receptor , physics , quantum mechanics , gene
SeveralN -substituted erythromycylamines were evaluated for their ability to inhibit the binding of [14 C]erythromycin to ribosomes. The association and dissociation constants for the binding of each compound toEscherichia coli ribosomes were determined. These studies have resulted in the development of three types of probes for topological studies of the erythromycin-binding site and the ribosome: the chemically reactive bromoacetamido, the photoreactiveN -(2)-nitro-4-azidophenyl)glycinamido, and the fluorescent fluorescein isothiocyanate derivatives of 9(S)-erythromycylamine.