128. Lin, F. C. and R. M. Brown, Jr. 1989. Purification of cellulose synthase from Acetobacter xylinum. In: Cellulose and Wood -Chemistry and Technology, Ed. C. Schuerch. John Wiley and Sons, Inc. N. Y., 473-492.

128. Synopsis

Cellulose synthase was extracted with Triton X-100 from trypsinized membranes of Acetobacter xylinum. The enzyme was purified 96-foId by repeated cellulose entrapment. Polyacrylamide gel electrophoresis of the purified cellulose synthase showed two major bands, 83 kDa and 93 kDa. Retention on Concanavalin A-Sepharose column suggests that the cellulose synthase is a glycoprotein. The periodic acid-Schiff base method using dansyl hydrazine and labelling with fluorescein isothiocyanate-Concanavalin A showed that the 83 kDa polypeptide strongly fluoresced in comparison with the other band. After the addition of trypsin, the purified enzyme still maintained its activity; however, only the 83 kDa polypeptide remained in the gel while the other polypeptide was degraded. These results strongly suggest that the 83 kDa polypeptide is an essential component of the cellulose synthase.

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Last modified 27 October 2005.
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