Purification and Molecular Analysis of an Extracellular γ-Glutamyl Hydrolase Present in Young Tissues of the Soybean Plant

A polypeptide present in intercellular wash fluids of young leaves ofGlycine maxhas been purified to electrophoretic homogeneity. The protein has been identified as γ-glutamyl hydrolase (GGH) based on the shared homology with a recently cloned cDNA from rat. The enzyme is present within the extracel...

Full description

Saved in:
Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 228; no. 1; pp. 1 - 6
Main Authors Huangpu, J., Pak, J.H., Graham, M.C., Rickle, S.A., Graham, J.S.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.11.1996
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:A polypeptide present in intercellular wash fluids of young leaves ofGlycine maxhas been purified to electrophoretic homogeneity. The protein has been identified as γ-glutamyl hydrolase (GGH) based on the shared homology with a recently cloned cDNA from rat. The enzyme is present within the extracellular space of young leaves and a portion is bound to the cell wall. Northern and Western analysis confirm that this polypeptide is expressed only in young (1-15 d old) leaf, stem and root tissue and is therefore expressed under a strict developmental program. The primary sequence of γ-glutamyl hydrolase shares amino acid identity with a cDNA clone from rat and two partially sequenced cDNAs fromArabidopsis.Although the completein vivofunction of γ-glutamyl hydrolase in plants is unclear, it is known that the protein plays a critical role in folate metabolism and therefore likely in meeting the physiological demands of growing plant tissues.
Bibliography:9701356
F60
F30
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1996.1608