Author:
Fan Der-Fong,Maclachlan G. A.
Abstract
Applied indoleacetic acid (10−4 – 10−6 M) increased elongation and the amount and specific activity of cellulase in sections detached from the epicotyl of Pisum sativum L. var. Alaska. Actinomycin D (20 μg/ml) inhibited growth and the capacity of sections for synthesizing protein from absorbed 14C-leucine. At the same time it caused cellulase levels to decrease at a rate which indicated a half-life for the enzyme of less than 24 h. Pea cellulase was most stable in vitro between pH 6 and 7; at or below pH 5 its rate of denaturation was comparable to its turnover rate in vivo. Fractionation of sections yielded wall preparations which contained cellulase at a higher specific activity than particles or supernatant. It is concluded that cellulase is synthesized in excised sections by an auxin-regulated mechanism. It is proposed that the enzyme is transported to the wall where it may promote elongation and eventually become denatured.
Publisher
Canadian Science Publishing
Cited by
60 articles.
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