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Plant and Cell Physiology, 1985, Vol. 26, No. 6 995-1001
© 1985


Article

Changes in the Activities of Various Glycosidases during Carrot Cell Elongation in a 2,4-D-Free Medium

Hiroshi Masuda1, Yoshihiro Ozeki, Shin-ichi Amino and Atsushi Komamine2

Department of Botany, Faculty of Science, University of Tokyo Tokyo 113, Japan

2 Present address and reprint requests: Biological Institute, Tohoku University, Sendai 980, Japan

Changes in the activities of some glycosidases were studied in carrot suspension cultures with and without 2,4-D. Remarkable cell elongation occurs in a medium without 2,4-D, while few cells elongate in a medium containing it. Glycosidases were fractionated into soluble, ionically wall-bound, tightly wall-bound and extracellular enzymes. The optimum pHs of all the ionically bound glycosidases were in an acidic range, 4.4–5.0.

The activities of the ionically and tightly bound ß-xylosidases and ß-galactosidases were higher in elongating than in non-elongating cells. Furthermore, the activities of these enzymes increased with cell elongation during culture, suggesting that they may play important roles in cell elongation. Higher activities of soluble and cell wall-bound ß-glucosidase and {alpha}-mannosidase were found in non-elongating rather than in elongating cells. The activities of all soluble glycosidases except ß-xylosidase were also higher in non-elongating cells. Only ß-xylosidase and ß-galactosidase activities were detectable in the medium of the elongation culture.

1 Present address: Department of Agricultural Chemistry, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido 080, Japan.


(Received November 14, 1984; Accepted May 20, 1985)
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