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PMID: 6797402 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The location of arabinosyl:hydroxyproline transferase in the membrane system of potato tissue culture cells.

The Biochemical journal ·Vol. 195 ·No. 3 ·1981-06-01 ·Pages 661-7

Owens RJ, Northcote DH

Abstract

Incubation of a particulate preparation from potato tissue culture cells with UDP-beta-L-[1-3H] arabinose yielded a glycoprotein fraction containing labelled material with the characteristics of hydroxyproline arabinosides. The sugar-protein linkage was resistant to hot alkaline hydrolysis, and the hydrolytic products showed similar electrophoretic and chromatographic behavior to authentic hydroxyproline-arabinosides prepared from potato tissue culture cell walls. Incorporation of arabinose into glycoprotein was stimulated by the addition of de-arabinosylated potato lectin. The product of the incubation co-migrated with native potato lectin on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The subcellular distribution of the arabinosyl-transferase was investigated by fractionating potato tissue culture membranes on a discontinuous sucrose gradient in the presence or absence of Mg2+. Under both fractionation conditions the highest specific activity of the enzyme was found in the Golgi-enriched fraction. The results are discussed in relation to the synthesis of the hydroxy-proline-rich glycoprotein component of plant cell walls.

MeSH Terms
Arabinose/metabolism Cell Membrane/drug effects,enzymology Cells, Cultured Edetic Acid/pharmacology Glycosides/metabolism Hydroxyproline/analogs & derivatives,metabolism Lectins/pharmacology Magnesium/pharmacology Pentosyltransferases/metabolism Plant Lectins Plants/drug effects,enzymology Subcellular Fractions/drug effects,enzymology
Chemicals
Glycosides Lectins Plant Lectins Edetic Acid Arabinose Pentosyltransferases arabinosyl-hydroxyproline transferase Magnesium Hydroxyproline
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Owens R J
Northcote D H
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31 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1950661
Published
1981-06-01
Pages
661-7
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1162938
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1950661 PMC Full Text View journal details
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