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...
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Published in: | Biochemical and biophysical research communications Vol. 228; no. 1; pp. 1 - 6 |
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Main Authors: | , , , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
Elsevier Inc
01-11-1996
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Subjects: | |
Online Access: | Get full text |
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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. |
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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 |