CHITINASE IN BEAN-LEAVES - INDUCTION BY ETHYLENE, PURIFICATION, PROPERTIES, AND POSSIBLE FUNCTION
CHITINASE IN BEAN-LEAVES - INDUCTION BY ETHYLENE, PURIFICATION, PROPERTIES, AND POSSIBLE FUNCTION
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DOI:
10.1007/bf00394536
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发表时间:
1983-01-01
期刊:
影响因子:
4.3
通讯作者:
VOGELI, U
中科院分区:
文献类型:
--
作者:
BOLLER, T;GEHRI, A;VOGELI, U
Ethylene induced an endochitinase in primary leaves of P. vulgaris L. The enzyme formed chitobiose and higher chitin oligosaccharides from insoluble, colloidal or regenerated chitin. Less than 5% of the total chitinolytic activity was detected in an exochitinase assay proposed by Abeles et al. (1970) for ethylene-induced chitinase. In ethylene-treated plants, chitinase activity started to increase after a lag of 6 h and was induced 30-fold within 24 h. Exogenously supplied ethylene at 1 nl ml-1 was sufficient for half-maximal induction, and enhancement of the endogenous ethylene formation also enhanced chitinase activity. Cycloheximide prevented the induction. Among various hydrolases tested, only chitinase and, to a lesser extent, .beta.-1,3-glucanase were induced by ethylene. Induction of chitinase by ethylene occurred in many different plant species. Ethylene-induced chitinase was purified by affinity chromatography on a column of regenerated chitin. Its apparent MW obtained by sodium dodecyl sulfate-gel electrophoresis was 30,000; the MW determined from filtration through Sephadex G-75 was 22,000. The purified enzyme attacked chitin in isolated cell walls of Fusarium solani. It also acted as a lysozyme when incubated with Micrococcus lysodeikticus. Apparently, ethylene-induced chitinase functions as a defense enzyme against fungal and bacterial invaders.