Studies on the Oxidative Fraction of Rabbit Muscle Glyceraldehyde-3-phosphate Dehydrogenase. Influence of Ligands on Its Obtention Enzymic Properties
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1970.tb01073.x/fullpdf
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1. Separation of Oxidative from Phosphorylative Activity by Proteolysis of Glyceraldehyde-3-Phosphate Dehydrogenase*
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3. Metabolic control and structure of glycolytic enzymes. VII. Destabilization and inactivation of yeast glyceraldehyde 3-phosphate dehydrogenase by adenosine phosphates and chymotrypsin
4. CRYSTALLINE d-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM RABBIT MUSCLE
5. CRYSTALLINE ALDOLASE
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2. Étude comparative de la modification chimique des groupes sulfhydryles des glycéraldéhyde-3-phosphate déshydrogénases de levure et de muscle de lapin;Biochimie;1982-07
3. Structure and Reactive Relationship in Glyeeraledehyde-3-Phosphate Dehydrogenase. Dinitrophenylation of Cysteine Residues of Yeast and Rabbit Muscle Enzymes;European Journal of Biochemistry;1981-10
4. Role of Lysine-183 in d-Glyceraldehyde-3-Phosphate Dehydrogenases. Properties of the N-Acetylated Yeast, Sturgeon Muscle and Rabbit Muscle Enzymes;European Journal of Biochemistry;1978-02
5. An investigation of the nicotinamide-adenine dinucleotide-induced ‘tightening’ of the structure of glyceraldehyde 3-phosphate dehydrogenase;Biochemical Journal;1976-07-01
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