Effects of a protease inhibitor on biosynthesis of Escherichia coli proteins.
A protease inhibitor, tosyl-L-lysine chloromethylketone, altered the composition of newly synthesized protein in Escherichia coli; a significant portion of the proteins synthesized sedimented rapidly, presumably forming aggregates of the abnormal proteins. Protein I of the outer membrane was only slightly synthesized under these conditions.
D000590:Amino Acid Chloromethyl Ketones / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000032:analysis / Q000096:biosynthesis*; D002498:Centrifugation; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D008565:Membrane Proteins / Q000032:analysis / Q000096:biosynthesis*; D014107:Tosyllysine Chloromethyl Ketone / Q000494:pharmacology*
D000590:Amino Acid Chloromethyl Ketones; D001426:Bacterial Proteins; D008565:Membrane Proteins; D014107:Tosyllysine Chloromethyl Ketone