Use of affinity chromatography for the quantitative study of acceptor–ligand interactions: the lactose synthetase system (Short Communication)
TLDR
From the effects of N-acetyl-d- glucosamine and d-glucose on the elution of the A protein of human lactose synthetase from a column of Sepharose-alpha-lactalbumin, values of 200m(-1) and 0.57m(- 1) are deduced for the association constants describing the interaction between the enzyme and the respective monosaccharides.Abstract:
From the effects of N-acetyl-d-glucosamine and d-glucose on the elution of the A protein of human lactose synthetase from a column of Sepharose–α-lactalbumin, values of 200m−1 and 0.57m−1 are deduced for the association constants describing the interaction between the enzyme and the respective monosaccharides.read more
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Journal ArticleDOI
Frontal affinity chromatography: theory for its application to studies on specific interactions of biomolecules.
TL;DR: Frontal analysis in affinity chromatography provides information almost identical to that obtainable by enzyme kinetic studies, especially for complicated systems where it has been difficult to find an appropriate method.
Journal ArticleDOI
Metal-ion binding and the molecular conformational properties of alpha lactalbumin.
TL;DR: This review is directed toward critically examining and integrating the present knowledge of the properties of alpha lactalbumin, particularly the relationship between metal-ion binding and conformational state, and how these might relate to its biological function.
Journal ArticleDOI
The kinetic mechansim of bovine milk galactosyltransferase. The role of alpha-lactalbumin.
TL;DR: Dissociation constants for UDP-galactose, acceptor substrates, and alpha-lactalbumin from the appropriate complexes have been calculated and are in good agreement with those obtained independently by nonkinetic methods, providing additional support for the proposed random equilibrium mechanism.
Journal ArticleDOI
Protein interaction with immobilized ligands: quantitative analyses of equilibrium partition data and comparison with analytical chromatographic approaches using immobilized metal affinity adsorbents.
TL;DR: The results support the validity and utility of equilibrium binding data analyzed according to the equations outlined by Scatchard and others as an alternative to analytical chromatographic methods.
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