The binding of oxidized and reduced nicotinamide adenine-dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase.
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Allosteric Regulation↗
Biomedical subjects
K Kirschner
Publications and source records attributed to K Kirschner.
Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. I. Equilibrium and temperature-jump studies at pH 8-5 and 40 degrees C.
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Dialysis↗
Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. II. Stopped-flow studies at pH 8-5 and 40 degrees C.
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Catalysis↗
X-ray small-angle scattering of yeast glyceraldehyde-3-phosphate dehydrogenase as a function of saturation with nicotinamide-adenine-dinucleotide.
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Chemical Phenomena↗
[Structural flexibility and enzyme function].
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Binding Sites↗
Recent advances in the study of biological systems with rapid reaction techniques.
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Journal Article↗
X-ray small-angle scattering of yeast glyceraldehyde-3-phosphate dehydrogenase as a function of saturation with nicotinamide-adenine-dinucleotide.
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Journal Article↗
[Purity criteria for the crystallizable isoenzyme of D-glyceraldehyde-3-phosphate dehydrogenase from baker's yeast].
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Chromatography, Ion Exchange↗
Allosteric regulation of enzyme activity. An introduction to the molecular basis of and the experimental approaches to the problem.
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Binding Sites↗
[Regulation of enzyme activity].
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Binding Sites↗
The binding of nicotinamide-adenine dinucleotide to yeast d-glyceraldehyde-3-phosphate dehydrogenase: temperature-jump relaxation studies on the mechanism of an allosteric enzyme.
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Journal Article↗
Socially-assisted dying and people with disabilities: some emerging legal, medical, and policy implications.
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Attitude of Health Personnel↗