Activity-based protein profiling of hydrolytic enzymes induced by gibberellic acid in isolated aleurone layers of malting barley.

Autor: Daneri-Castro SN; Faculty of Agriculture and Environment, Plant Breeding Institute, University of Sydney, Eveleigh, Australia., Chandrasekar B; The Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, UK., Grosse-Holz FM; The Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, UK., van der Hoorn RA; The Plant Chemetics Laboratory, Department of Plant Sciences, University of Oxford, UK., Roberts TH; Faculty of Agriculture and Environment, Plant Breeding Institute, University of Sydney, Eveleigh, Australia.
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 2016 Sep; Vol. 590 (17), pp. 2956-62. Date of Electronic Publication: 2016 Aug 04.
DOI: 10.1002/1873-3468.12320
Abstrakt: During barley germination, the aleurone layer secretes most of the enzymes required to degrade the endosperm, many of which are yet to be characterized. We used activity-based protein profiling (ABPP) to detect a range of active enzymes extracted from aleurone layers isolated from grains of a commercial malting barley variety incubated with or without gibberellic acid (GA). Enzymes found to be induced by GA were putative aleurains, cathepsin-B-like proteases and serine hydrolases. By using an inhibitory sugar panel, a specific active retaining β-glycosidase in the barley aleurone was identified as a putative xylanase. Our results show that ABPP can be used rapidly to identify a variety of active enzyme isoforms in cereal aleurone without the need for enzyme purification.
(© 2016 Federation of European Biochemical Societies.)
Databáze: MEDLINE
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