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Appl Environ Microbiol. 1969 March; 17(3): 467-472
Copyright © 1969 American Society for Microbiology. All Rights Reserved.
Department of Microbiology, Schools of Medicine and Veterinary Medicine, University of Missouri, Columbia, Missouri 65201
Department of Veterinary Microbiology, Schools of Medicine and Veterinary Medicine, University of Missouri, Columbia, Missouri 65201
ABSTRACT
Fractionation of leptospiral lipase by CsCl density gradients and G-200 Sephadex chromatography yielded five active protein peaks. Two were obtained from the density gradients and three from G-200 Sephadex columns. Esterase activity of these fractions was demonstrated by electrophoretic examination. Several protein bands were visible when disc electrophoresis was performed on the respective fractions. Lipolytic and esterolytic activities were both present, and the overlapping of these activities was discussed.
1 Present address: Department of Medicine, University of Illinois, Chicago, Ill.
2 Present address: Veterinary Medicine, Walter Reed Army Institute of Research, Washington, D.C.
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