Fulminating lactose-positive Vibrio septicemia.

Recently cases of tissue invasion by as yet unnamed marine vibrios which were morphologically and biochemically similar to both Vibrio parahemolyticus and V. alginolyticus, but not identical with either of them, have been described. We have seen a patient who had serious widespread tissue infection with a halophilic, Gram-negative bacterium which was isolated from blood and leg lesions. The organism had the characteristics of the genus Vibrio, and lactose fermentation and ONPG reactions were positive. It also had a lower tolerance for sodium chloride in the nutrient broth compared with the above two vibrios. The isolate seems identical to the lactose positive (L+) Vibrio described by HOLLIS et al. (1976). Tissue infection resulting in severe necrotizing cellulitis and vasculitis was demonstrated at autopsy.

Purification and properties of mycodextranase from Streptomyces sp. J-13-3.

An enzyme hydrolyzing nigeran (alternating alpha-1,3- and alpha-1,4-linked glucan) was purified from the culture filtrate of Streptomyces sp. J-13-3, which lysed the cell wall of Aspergillus niger, by percipitation with ammonium sulfate and column chromatographies on DEAE-Sephadex A-50, CM-Sephadex C-50, chromatofocusing, and Sephadex G-100. The final preparation was homogenous in polyacrylamide gel electrophoresis (PAGE). The molecular weight of the enzyme was 68,000 by SDS-PAGE and gel filtration. The optimum pH and temperature for the enzyme activity were 6.0 and 50 degrees C, respectively. The enzyme was stable in the pH range from 6.0 to 8.0 and up to 50 degrees C. The enzyme activity was inhibited significantly by Hg+, Hg2+, and p-chloromercuribenzoic acid. The Km (mg/ml) for nigeran was 3.33. The enzyme specifically hydrolyzed nigeran into nigerose and nigeran tetrasaccharide by an endo-type of action, indicating it to be a mycodextranase (EC 3.2.1.61) that splits only the alpha-1,4-glucosidic linkages in nigeran.