Axial Distribution of Glycosidases in Relation to Cellular Growth and Ageing inPisum sativumRoot
- 1 August 1985
- journal article
- research article
- Published by Oxford University Press (OUP) in Journal of Experimental Botany
- Vol. 36 (8) , 1267-1274
- https://doi.org/10.1093/jxb/36.8.1267
Abstract
Tanimoto, E. 1985. Axial distribution of glycosidases in relation to cellular growth and ageing in Pisum sativum root.—J. exp. Bot. 36: 1267–1274. Eight glycosidase activities were measured in relation to cellular growth and ageing along the axis of pea roots. The highest activities of β-D-fucosidase and β-D-glucosidase were in the apical 1.0 mm segment containing the root cap and meristem. Activities of α-L-arabinosidase, α-D-mannosidase, β-D- galactosidase, α-D-glucosidase and β-D-xylosidase were highest in the segment between 1 and 2 mm from the tip and containing young elongating cells with high growth potential. The activity of α-D-galactosidase was high between 1 and 2 mm from the root tip, decreasing to a minimum 4-5 mm from the tip and increasing again up to the base of root. This distribution of enzyme activities relative to the root tip remained unchanged during 28 h while the root length doubled. No α-L--fucosidase, β-L-fucosidase and α-D-xylosidase activities were detected.Keywords
This publication has 7 references indexed in Scilit:
- β-Galactosidases in Ripening TomatoesPlant Physiology, 1983
- Glycosidases from Cotyledons ofPisum sativumL.Journal of Experimental Botany, 1980
- Degradation of Cell Wall Polysaccharides during Tomato Fruit RipeningPlant Physiology, 1979
- The Relationship of Some Glycosidases to the Endogenous and IAA-induced Growth of Light-grown Cucumber HypocotylsPhysiologia Plantarum, 1979
- Isolation and Purification of an α-Mannosidase from Coleoptiles of Avena sativaPlant Physiology, 1977
- Correlation, between β-galactosidase and auxin-induced elongation growth in etiolated pea stemsPlant and Cell Physiology, 1976
- Inhibition of glycosidases by aldonolactones of corresponding configuration. The C-4- and C-6-specificity of β-glucosidase and β-galactosidaseBiochemical Journal, 1967