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.
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.