Beta-1, 3-glucan synthase from Lilium longiflorum pollen

A particulate fraction from pollen tubes and ungerminated pollen of Lilium longiflorum incorporated 14C-glucose from UDP-glucose-14C into a lipid fraction and into β-1,3-glucan. Partial hydrolysis of the glucan yielded laminaribiose as the only radioactive disaccharide. The preferred substrate was U...

Full description

Saved in:
Bibliographic Details
Published in:Plant physiology (Bethesda) 1975-07, Vol.56 (1), p.83-87
Main Authors: Southworth, D, Dickinson, D.B
Format: Article
Language:English
Subjects:
Cell walls
Enzyme activity
Enzyme substrates
Enzymes
Germination
Glucans
Particulate matter
Pollen
Pollen tubes
Polysaccharides
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A particulate fraction from pollen tubes and ungerminated pollen of Lilium longiflorum incorporated 14C-glucose from UDP-glucose-14C into a lipid fraction and into β-1,3-glucan. Partial hydrolysis of the glucan yielded laminaribiose as the only radioactive disaccharide. The preferred substrate was UDP-glucose, and enzyme activity was stimulated by glucose and by β-linked di- and trisaccharides. Enzyme from growing pollen tubes synthesized β-1,3-glucan more rapidly and produced a higher proportion of alkali-insoluble glucan than did enzyme from ungerminated pollen. The onset of pollen tube growth may be dependent on altered activity of β-1,3-glucan synthase.
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.56.1.83