Two immunologically different penicillin amidases synthetized by Escherichia coli PCM 271.
From Escherichia coli PCM 271 cells two penicillin amidases were separated by affinity chromatography on immunoadsorbent column. In cells grown in organic medium the activities of the amidase 1 and 2 were 30 and 70% respectively, whereas the activity of the amidase 1 in the cells grown in inorganic medium increased up to 98%. The amidase 1 migrated faster in polyacrylamide gel electrophoresis and was retained on DEAE-cellulose in 10 mM phosphate buffer, pH 8. No catalytic differences were demonstrated between the amidases.
D000581:Amidohydrolases / Q000096:biosynthesis*; D004926:Escherichia coli / Q000201:enzymology*; D007120:Immunochemistry; D010399:Penicillin Amidase / Q000096:biosynthesis* / Q000276:immunology / Q000302:isolation & purification
D000581:Amidohydrolases; D010399:Penicillin Amidase