Characterization of Purified Staphylococcal Lipase1
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چکیده
منابع مشابه
The Characterization of Staphylococcal Toxins
The continuous flow paper electrophoretic methods used to isolate alpha hemolysin are presented. The purity of the alpha hemolysin preparation is demonstrated by double agar diffusion, immunoelectrophoretic, and ultracentrifugation techniques. Indirect evidence of purity is provided by the fact that rabbit immunized with purified alpha hemolysin produced detectable antibody only to alpha hemoly...
متن کاملAmmonium sulfate coprecipitation antibody determination with purified staphylococcal enterotoxins.
The ammonium sulfate coprecipitation technique of Farr was applied in a study of the purified enterotoxins of Staphylococcus aureus. Ammonium sulfate coprecipitation of iodine-131-labeled enterotoxins A, B, and C, with the use of a 1.6 m concentration of (NH(4))(2)SO(4), revealed differences in the antigen-binding capacity of normal and immune rabbit sera for the enterotoxins. The coprecipitati...
متن کاملFurther characterization of staphylococcal gamma-hemolysin.
It was confirmed that staphylococcal gamma-hemolysin is composed of two separate proteins (gamma-lysin components I and II) which act synergistically. The molecular weights of the two components, determined by gel filtration, are 29,000 and 26,000, respectively, and their isoelectric points, determined by isoelectric focusing, are at pH 9.8 and 9.9. Both components are susceptible to the action...
متن کاملIsolation and characterization of a staphylococcal lipase.
A number of coagulase-negative staphylococci isolated from human skin were found to produce lipase. Lipolytic activity appeared in the growth medium during the stationary phase of growth but did not appear as a result of autolysis of the cells. Maximal lipase synthesis was obtained when the medium was adjusted to pH 7.5 before inoculation. The purified enzyme hydrolyzed tributyrin and tridecano...
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ژورنال
عنوان ژورنال: Applied Microbiology
سال: 1967
ISSN: 0003-6919
DOI: 10.1128/aem.15.3.480-483.1967