Micelles of pyridoxal-5′-phosphate Schiff bases — An improved model for the B6 site of glycogen phosphorylase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference22 articles.
1. The isolation of pyridoxal-5-phosphate from crystalline muscle phosphorylase
2. On the Role of Pyridoxal 5'-Phosphate in Phosphorylase. II. Resolution of Rabbit Muscle Phosphorylase b*
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4. Chemical and Biological Aspects of Pyridoxal Catalysis;Fischer,1963
5. On the Role of Pyridoxal 5'-Phosphate in Phosphorylase. I. Absence of Classical Vitamin B6—dependent Enzymatic Activities in Muscle Glycogen Phosphorylase*
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1. Pyridoxal Phosphate and Hepatocyte Growth Factor Prevent Dialysate-Induced Peritoneal Damage;Journal of the American Society of Nephrology;2004-11-24
2. Substitution of Pyridoxal 5′-Phosphate in the O-Acetylserine Sulfhydrylase from Salmonella typhimurium by Cofactor Analogs Provides a Test of the Mechanism Proposed for Formation of the α-Aminoacrylate Intermediate;Journal of Biological Chemistry;1996-10
3. Function of pyridoxal 5'-phosphate in glycogen phosphorylase: fluorine-19 NMR and kinetic studies of phosphorylase reconstituted with 6-fluoropyridoxal and 6-fluoropyridoxal phosphate;Biochemistry;1986-04-01
4. Coenzyme catalyses in micelles, polymers and host molecules;Progress in Polymer Science;1982-01
5. Spectrophotometric titrations of micellar Schiff's bases prepared from pyridoxal 5′-phosphate;International Journal of Biological Macromolecules;1981-12
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