Reaction of rabbit muscle apo-glyceraldehyde-3-p- dehydrogenase with pyridoxal-5′-phosphate
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(73)80124-3/fullpdf
Reference19 articles.
1. S.P. Colowick J. van Eys J.H. Park Comprehensive biochemistry 14 1966 Elsevier Publ Amsterdam, London, New York 63
2. Binding and properties of NAD+ in glyceraldehydephosphate dehydrogenase from lobster-tail muscle
3. Coenzyme-induced Changes in the Optical Rotatory Dispersion Properties of Glyceraldehyde 3-Phosphate Dehydrogenase
4. Mechanism of nicotinamide-adenine dinucleotide binding to rabbit muscle glyceraldehyde 3-phosphate dehydrogenase
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2. Identification of a critical lysine residue at the active site in glyceraldehyde-3-phosphate dehydrogenase of Ehrlich ascites carcinoma cell;European Journal of Biochemistry;2001-12-01
3. Glyceraldehyde-3-phosphate dehydrogenase;Philosophical Transactions of the Royal Society of London. B, Biological Sciences;1981-06-26
4. Pyridoxal 5′-phosphate—A new physiological inhibitor of blood coagulation and platelet function;Biochemical Pharmacology;1979
5. Bacterial Racemization ofα-Amino-ε-caprolactam;Agricultural and Biological Chemistry;1977-08
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