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E A DELWICHE

Publications and source records attributed to E A DELWICHE.

At least 19 recordsLinked to original sources

DISTRIBUTION AND CHARACTERISTICS OF THE CATALASES OF LACTOBACILLACEAE.

Johnston, M. A. (Cornell University, Ithaca, N.Y.), and E. A. Delwiche. Distribution and characteristics of the catalases of Lactobacillaceae. J. Bacteriol. 90:347-351. 1965.-Certain strains of lactobacilli and pediococci incorporated hematin during growth, with the concomitant formation of cyanide- and azide-sensitive catalase. Three of five strains of lactobacilli and five of 25 strains of pediococci were capable of this biosynthesis. The pediococci required the heme component of blood, whereas the lactobacilli could incorporate the heme component in the form of purified and solubilized hemin or from blood. In all cases where inhibitor-sensitive enzyme was produced, it was accompanied by the production of inhibitor-insensitive enzyme. In the absence of hematin, only insensitive enzyme was obtained. Two catalase-positive strains of Streptococcus faecalis were found incapable of the synthesis of a heme-type enzyme, as was one member of the genus Leuconostoc. Iron and manganese in the growth medium stimulated the production of the insensitive catalase, but significant quantities of these metals could not be found in a purified enzyme preparation obtained from Lactobacillus plantarum. Aeration had little or no effect on growth, but it consistently doubled the amount of cyanide- and azide-resistant catalase. By means of conventional enzyme fractionation techniques, it was possible to separate the two different enzymes present in the cell-free extract of a strain of Pediococcus homari which had been grown in the presence of blood.

Azides↗

ISOLATION AND CHARACTERIZATION OF THE CYANIDE-RESISTANT AND AZIDE-RESISTANT CATALASE OF LACTOBACILLUS PLANTARUM.

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

Animals↗