JBC Ideal method for primary cell transfection

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Volume 272, Number 1, Issue of January 3, 1997 pp. 479-485
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Biosynthesis of Teichuronic Acid in the Bacterial Cell Wall
PURIFICATION AND CHARACTERIZATION OF THE GLUCOSYLTRANSFERASE OF MICROCOCCUS LUTEUS

(Received for publication, July 3, 1996, and in revised form, October 10, 1996)

Lingyi Deng and John S. Anderson

From the Department of Biochemistry, College of Biological Sciences, University of Minnesota, St. Paul, Minnesota 55108

This report describes what is, to our knowledge, the first purification to near homogeneity of an enzyme involved in the biosynthesis of the teichuronic acid of Micrococcus luteus cell walls. The glucosyltransferase of M. luteus, which participates in the biosynthesis of teichuronic acid, was solubilized from cytoplasmic membrane fragments by extraction with buffer solutions containing the detergents Thesit (dodecyl alcohol polyoxyethylene ether; 1 mg/ml) and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (0.5 mg/ml). The detergent-solubilized enzyme was purified 150-fold, with a recovery of 13% by adsorbent column chromatography, ion-exchange chromatography, gel filtration, and preparative nondenaturing gradient polyacrylamide gel electrophoresis. On the basis of its mobility on native gradient gel, the glucosyltransferase was estimated to have a molecular mass of 440 kDa. The purified native enzyme was a multisubunit protein consisting of subunits of two sizes; their molecular masses were determined to be 52.5 and 54 kDa, respectively, by observation of the mobility of the protein bands in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric point of the enzyme was ~5.


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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.