Elaine M Wise

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The principal autolytic enzyme activity of the cell sap of Staphylococcus aureus H has been purified 400-fold. It is an N-acetylmuramyl-l-alanine amidase. This enzyme has a molecular weight of 8 to 10 x 10(5), a pH optimum of 7.3, an ionic strength optimum of 0.16 m and a K(m) of 10(-3)m murein repeating units.
Staphylococcus aureus strain H has an autolytic activity which can be found in the cell wall but is most easily obtained from high-speed supernatant fractions of broken-cell preparations. As measured either turbidimetrically or radioactively, this activity is much greater on murein extracted from penicillin-treated cells than on murein extracted from normal(More)
Several natural isolate E. coli strains highly resistant to sulfonamides and antibiotics are shown to contain a sulfonamide-resistant dihydropteroate synthase (2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase, EC 2.5.1.15) in addition to the normal sensitive enzyme.(More)
Adenosine 3':5'-cyclic monophosphate added to exponentially growing cells of Hemophilus influenzae strain Rd increases competence for transformation 100- to 10,000-fold. Cyclic AMP added to near-stationary or stationary cells does not increase competence over the high level normally found in the early stationary phase.