SUMMARY: A purification procedure for isocitrate lyase (ICL) is described. Thirteen mutants at the locus produced no detectable ICL activity either on sucrose as sole carbon source or in the presence of acetate. These mutants also produced little or no protein able to neutralize anti-ICL antibodies. Selection of revertants, able to grow on acetate as sole carbon source, from one of the mutants gave one class with moderately thermolabile and one with highly thermolabile ICL as well as apparently true revertants with ICL of wild-type stability. The mutants with highly labile ICL grew on acetate at 25° but not at 37°. One of the temperature-sensitive revertants was analysed genetically and shown to be due to further mutation within or close to itself.


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