Differentiation of Micrococcus luteus and Micrococcus varians on the Basis of Catalase Isoenzymes
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چکیده
منابع مشابه
Differentiation of Micrococcus luteus and Micrococcus varians on the basis of catalase isoenzymes.
Crude extracts prepared from four Micrococcus varians strains, 11 M. luteus strains and four laboratory isolates subsequently classified with M. luteus were assayed for catalase activity following electrophoresis on polyacrylamide gels. The enzyme patterns produced from the M. varians strains exhibited three catalase isoenzymes which were distinguished into two types of patterns depending upon ...
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Resting cells of Micrococcus luteus have been shown to remove strontium (Sr) from dilute aqueous solutions of SrCl(2) at pH 7. Loadings of 25 mg of Sr per g of cell dry weight were achieved by cells exposed to a solution containing 50 ppm (mg/liter) of Sr. Sr binding occurred in the absence of nutrients and did not require metabolic activity. Initial binding was quite rapid (<0.5 h), although a...
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A DNA-relaxing enzyme which catalyzes the conversion of superhelical DNA to a non-superhelical covalently closed form has been purified from Micrococcus luteus to near homogeneity by two chromatographic steps. The enzyme is a single polypeptide chain. As determined by sodium dodecyl sulfate - polyacrylamide gel electrophoresis and gel filtration on Sephadex G 150, the molecular weight is 115,00...
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Micrococcus luteus produced 29 muM riboflavin during growth on 6.5 mM pyridine but not during growth on other substrates. On the basis of the results of radiolabelling studies, riboflavin was not directly synthesized from pyridine. Pyridine may interfere with riboflavin biosynthesis or elicit a general stress response in M. luteus.
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An w protein capable of a concerted breaking and rejoining of DNA backbone bonds has been purified from Micrococcus luteus to homogeneity. The protein is a single polypeptide with a molecular weight of 120,000. It catalyzes the removal of superhelical turns from a highly negatively twisted DNA efficiently. The reaction requires Mg2+. In a medium containing 0.1 M K+, the enzyme acts in distribut...
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ژورنال
عنوان ژورنال: Journal of General Microbiology
سال: 1976
ISSN: 0022-1287
DOI: 10.1099/00221287-93-2-272