Protein hydration changes in the formation of the nicotinamide adenine dinucleotide complexes of glyceraldehyde 3-phosphate dehydrogenase of yeast. I. Buoyant densities, preferential hydrations, and fluorescence-quenching titrations. - Suppr | 超能文献

Protein hydration changes in the formation of the nicotinamide adenine dinucleotide complexes of glyceraldehyde 3-phosphate dehydrogenase of yeast. I. Buoyant densities, preferential hydrations, and fluorescence-quenching titrations.

作者信息

Sloan D L, Velick S F

出版信息

J Biol Chem. 1973 Aug 10;248(15):5419-23.

Abstract

摘要

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Protein hydration changes in the formation of the nicotinamide adenine dinucleotide complexes of glyceraldehyde 3-phosphate dehydrogenase of yeast. I. Buoyant densities, preferential hydrations, and fluorescence-quenching titrations.

J Biol Chem. 1973 Aug 10;248(15):5419-23.

2

Protein hydration changes in the formation of the nicotinamide adenine dinucleotide complexes of glyceraldehyde 3-phosphate dehydrogenase of yeast. II. The spin lattice relaxation of solvent water protons.

J Biol Chem. 1973 Aug 10;248(15):5424-7.

3

Energetics of the cooperative and noncooperative binding of nicotinamide adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase at pH 6.5 and pH 8.5. Equilibrium and calorimetric analysis over a range of temperature.烟酰胺腺嘌呤二核苷酸在pH 6.5和pH 8.5条件下与酵母甘油醛-3-磷酸脱氢酶协同及非协同结合的能量学。在一定温度范围内的平衡和量热分析。

Biochemistry. 1977 Feb 8;16(3):436-45. doi: 10.1021/bi00622a015.

4

[Fluorimetric determination of the binding of nicotinamide-adenine dinucleotide fragments with D-glyceraldehyde-3-phosphate dehydrogenase].[荧光法测定烟酰胺腺嘌呤二核苷酸片段与3-磷酸甘油醛脱氢酶的结合]

Dokl Akad Nauk SSSR. 1975 Dec 21;225(6):1438-41.

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Glyceraldehyde-3-phosphate dehydrogenase catalyzed hydration of the 5-6 double bond of reduced beta-nicotinamide adenine dinucleotide (betaNADH). Formation of beta-6-hydroxy-1,4,5,6-tetrahydronicotinamide adenine dinucleotide.

Biochemistry. 1974 Nov 5;13(23):4685-94. doi: 10.1021/bi00720a002.

6

The binding of oxidized and reduced nicotinamide adenine-dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase.

Eur J Biochem. 1972 Mar 27;26(2):220-36. doi: 10.1111/j.1432-1033.1972.tb01760.x.

7

Relationship between fluorescence and conformation of epsilonNAD+ bound to dehydrogenases.与脱氢酶结合的εNAD⁺的荧光与构象之间的关系。

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8

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.烟酰胺腺嘌呤二核苷酸与酵母甘油醛-3-磷酸脱氢酶的协同结合。I. 在pH 8.5和40℃条件下的平衡和温度跃变研究

J Mol Biol. 1971 May 28;58(1):29-50. doi: 10.1016/0022-2836(71)90230-0.

9

The binding of NAD+ to rabbit muscle glyceraldehyde-3-phosphate dehydrogenase studied by protein fluorescence quenching.

Biochim Biophys Acta. 1971 Apr 14;235(1):27-31. doi: 10.1016/0005-2744(71)90029-5.

10

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.烟酰胺腺嘌呤二核苷酸与酵母甘油醛-3-磷酸脱氢酶的协同结合。II. pH 8.5和40℃下的停流研究。

J Mol Biol. 1971 May 28;58(1):51-68. doi: 10.1016/0022-2836(71)90231-2.

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