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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1992-11-13
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pubmed:databankReference |
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pubmed:abstractText |
A new member of the barley (1-->3)-beta-glucan glucanohydrolase family of enzymes has been purified from extracts of germinated grain and young seedlings by fractional precipitation with ammonium sulphate, ion-exchange chromatography, chromatofocussing and gel-filtration chromatography. The enzyme, which has been designated (1-->3)-beta-glucanase isoenzyme GIII, is a basic protein with an apparent molecular mass of 32 000 Da. Oligosaccharide products released by the enzyme during hydrolysis of the (1-->3)-beta-glucan, laminarin, indicate that the enzyme is an endohydrolase. A 2349-bp fragment of barley genomic DNA has been isolated and identified as the gene encoding the (1-->3)-beta-glucanase isoenzyme GIII. The open reading frame encoding the isoenzyme is interrupted by a single intron of 180 bp that splits a codon in the putative signal-peptide region. Northern-blot analyses with gene-specific probes indicate that the (1-->3)-beta-glucanase isoenzyme GIII mRNA accumulates in developing leaves; no mRNA transcripts were detected in the aleurone or scutellum of germinated grain, or in mature vegetative tissues. Although plant (1-->3)-beta-glucanases are generally classified as 'pathogenesis-related' proteins, the physiological function of the barley (1-->3)-beta-glucanase isoenzyme GIII is unclear.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-2956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
209
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
103-9
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:1396688-Amino Acid Sequence,
pubmed-meshheading:1396688-Base Sequence,
pubmed-meshheading:1396688-Blotting, Northern,
pubmed-meshheading:1396688-Chromatography,
pubmed-meshheading:1396688-Cloning, Molecular,
pubmed-meshheading:1396688-DNA,
pubmed-meshheading:1396688-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1396688-Gene Expression,
pubmed-meshheading:1396688-Genes, Plant,
pubmed-meshheading:1396688-Glucan 1,3-beta-Glucosidase,
pubmed-meshheading:1396688-Hordeum,
pubmed-meshheading:1396688-Hydrogen-Ion Concentration,
pubmed-meshheading:1396688-Isoenzymes,
pubmed-meshheading:1396688-Molecular Sequence Data,
pubmed-meshheading:1396688-Molecular Weight,
pubmed-meshheading:1396688-Plasmids,
pubmed-meshheading:1396688-RNA, Messenger,
pubmed-meshheading:1396688-Restriction Mapping,
pubmed-meshheading:1396688-Transcription, Genetic,
pubmed-meshheading:1396688-beta-Glucosidase
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pubmed:year |
1992
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pubmed:articleTitle |
Purification, characterization and gene structure of (1-->3)-beta-glucanase isoenzyme GIII from barley (Hordeum vulgare).
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pubmed:affiliation |
Department of Biochemistry, La Trobe University, Victoria, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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