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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1998-4-23
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pubmed:abstractText |
The affinity of potato tuber starch-branching enzyme-I (PSBE-I) for various linear malto-oligosaccharides, cyclodextrins, (CDs) and macromolecular alpha-glucans was investigated by alpha-glucan induced fluorescence quenching of intrinsic PSBE-I tryptophan residues and by affinity electrophoresis. alpha-Glucan binding was characterised by distinct shifts towards shorter wavelengths of the PSBE-I fluorescence emission spectrum and by concomitant reductions in fluorescence intensity. The magnitudes of both the maximum shift in emission spectrum and reduction in fluorescence intensity were dependent on the alpha-glucan ligands used. Maximum Kd for a range of linear malto-oligosaccharides analysed was 0.13 mM as found at a degree of polymerisation (DP) of 13. Large differences in dissociation constants were measured for CDs with DP 6 (alpha-CD, 6.0 mM), DP 7 (beta-CD, 0.25 mM) and DP 8 (gamma-CD, 0.67 microM). The high-molecular-mass alpha-glucans amylose and amylopectin, both substrates for PSBE-I, showed apparent affinities of 0.018 and 0.066 mg/ml, respectively. Small linear and cyclic oligosaccharides competed with amylopectin in the affinity electrophoresis system and they were also competitive inhibitors for PSBE-I activity. The affinities for oligosaccharides as measured by competition were, however, about 10-fold lower than as measured by fluorescence quenching suggesting the existence of a separate oligosaccharide binding site on PSBE-I. Affinity electrophoresis revealed multiform heterogeneity in the enzyme preparation with respect to alpha-glucan interaction.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1,4-alpha-Glucan Branching Enzyme,
http://linkedlifedata.com/resource/pubmed/chemical/Amylopectin,
http://linkedlifedata.com/resource/pubmed/chemical/Amylose,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclodextrins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucans,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/maltohexaose
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
252
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
331-8
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:9523705-1,4-alpha-Glucan Branching Enzyme,
pubmed-meshheading:9523705-Amylopectin,
pubmed-meshheading:9523705-Amylose,
pubmed-meshheading:9523705-Binding, Competitive,
pubmed-meshheading:9523705-Binding Sites,
pubmed-meshheading:9523705-Cyclodextrins,
pubmed-meshheading:9523705-Glucans,
pubmed-meshheading:9523705-Kinetics,
pubmed-meshheading:9523705-Oligosaccharides,
pubmed-meshheading:9523705-Plant Proteins,
pubmed-meshheading:9523705-Protein Binding,
pubmed-meshheading:9523705-Solanum tuberosum,
pubmed-meshheading:9523705-Spectrometry, Fluorescence,
pubmed-meshheading:9523705-Tryptophan
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pubmed:year |
1998
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pubmed:articleTitle |
Alpha-glucan binding of potato-tuber starch-branching enzyme I as determined by tryptophan fluorescence quenching, affinity electrophoresis and steady-state kinetics.
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pubmed:affiliation |
Cooperative Research Centre for Plant Science, Canberra, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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