Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.

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Novel carbohydrate binding modules in the surface anchored α-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut.

P2860

Q48301307-CDB040BB-E300-450D-93C3-FDF00B34829E

P2860

Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.

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http://www.wikidata.org/entity/Q50912779

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.

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Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.

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Item

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Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.

@en

Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.

@nl

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Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.

@en

Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.

@nl

P1476

Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.

@en

P2860

A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: application to components of the Escherichia coli lactose operon regulatory system

Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis

Electrophoresis buffers for polyacrylamide gels at various pH

Surface binding sites in amylase have distinct roles in recognition of starch structure motifs and degradation.

A secondary xylan-binding site enhances the catalytic activity of a single-domain family 11 glycoside hydrolase.

Alpha-glucan binding of potato-tuber starch-branching enzyme I as determined by tryptophan fluorescence quenching, affinity electrophoresis and steady-state kinetics.

Interaction of polysaccharides with the N-terminal cellulose-binding domain of Cellulomonas fimi CenC. 1. Binding specificity and calorimetric analysis.

Plant α-glucan phosphatases SEX4 and LSF2 display different affinity for amylopectin and amylose.

An efficient arabinoxylan-debranching α-L-arabinofuranosidase of family GH62 from Aspergillus nidulans contains a secondary carbohydrate binding site.

Dissociation constants of glucan phosphorylases of rabbit tissues studied by polyacrylamide gel disc electrophoresis.

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119-127

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scholarly article

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10.1007/978-1-4939-6899-2_9

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P407

English

P478

1588

http://www.w3.org/2001/XMLSchema#string

P50

Casper Wilkens

Darrell W. Cockburn

Birte Svensson

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2017-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

28417364

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Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.

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P2860

P2860

Affinity Electrophoresis for Analysis of Catalytic Module-Carbohydrate Interactions.

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P1433

P1476

P2860

P304

P31

P356

P407

P478

P50

P577

P698

P356

P1433

P1476

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P304

P31

P356

P407

P478

P50

P577

P698