Isolation and Characterization of the Cyanide-Resistant and Azide-Resistant Catalase of Lactobacillus plantarum

摘要: Johnston, M. A. (Cornell University, Ithaca, N.Y.), and E. Delwiche. Isolation characterization of the cyanide-resistant azide-resistant catalase Lactobacillus plantarum. J. Bacteriol. 90:352–356. 1965.—Lactobacillus plantarum T-1403-5 has been shown to possess a very active cyanide- catalase. By means fractional ammonium sulfate precipitation, removal nucleic acids with protamine sulfate, adsorption on calcium phosphate gel, pH gradient chromatography diethylaminoethyl cellulose, “activity” was purified approximately 14-fold. The enzyme preparation insensitive heme poisons cyanide azide, metal chelating agents ethylenediaminetetraacetate o-phenanthroline, sulfhydryl binding agent p-chloromercuribenzoate. moved at uniform rate in electrophoretic field (isoelectric point, 4.7). ultraviolet-light absorption spectrum negative for heme-iron components, fluorescence measurements yielded results regard flavin components. Acriflavin Atabrine had no effect activity. nonheme displayed much broader range activity than control culture Escherichia coli azide-sensitive developed by L. NZ48 when grown presence preformed hematin. more resistant heat inactivation. No retention chromatographic column could be obtained Sephadex 200, nor separated from crystalline beef-liver gel filtration technique. Sedimentation centrifugal 144,000 × g 12 hr.