Studies on alkaline phosphatase, catalase and z-galactosidase in Vibrio el tor under normal and rifampicin resistant conditions.
Alkaline phosphate, catalase and beta-galactosidase activities of Vibrio et tor were decreased after acquisition of resistance towards rifampicin. Zn2+, Mn2+ and EDTA inhibited alkaline phosphatase which is most active with p-nitrophenylphosphate as substrate while Mg2+ was found to suppress alkaline phosphatase activity. Removal of EDTA however, restores the original activity. Rifampicin could not induce mutation of lactose nonfermenting Vibrio el for cells allowing them to grow on lactose as sole carbon source, z-galactosidase which is a constitutive enzyme in this case is repressed by glucose. This repression is overcome by cAMP.
D000469:Alkaline Phosphatase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002374:Catalase / Q000378:metabolism*; D003470:Culture Media; D046508:Culture Techniques; D004352:Drug Resistance, Microbial; D004492:Edetic Acid / Q000494:pharmacology; D005696:Galactosidases / Q000378:metabolism*; D005947:Glucose / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D012293:Rifampin / Q000494:pharmacology*; D014734:Vibrio cholerae / Q000201:enzymology*; D015032:Zinc / Q000494:pharmacology; D001616:beta-Galactosidase / Q000037:antagonists & inhibitors / Q000378:metabolism*
D003470:Culture Media; D008345:Manganese; D004492:Edetic Acid; D002374:Catalase; D000469:Alkaline Phosphatase; D005696:Galactosidases; D001616:beta-Galactosidase; D005947:Glucose; D015032:Zinc; D012293:Rifampin