Cooperativity in the interaction of glyceraldehyde 3-phosphate dehydrogenase with erythrocyte membranes
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference5 articles.
1. The Interaction of Glyceraldehyde 3-Phosphate Dehydrogenase with Human Erythrocyte Membranes
2. Specificity in the Association of Glyceraldehyde 3-Phosphate Dehydrogenase with Isolated Human Erythrocyte Membranes
3. The isolation and functional identification of a protein from the human erythrocyte ‘ghost’
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1. Kinetic and physico-chemical analysis of enzyme complexes and their possible role in the control of metabolism;Progress in Biophysics and Molecular Biology;1989
2. Changes in Conformational State of Glyceraldehyde-3-Phosphate Dehydrogenase Adsorbed on Phosphatidylinositol Liposomes;Electromagnetic Fields and Biomembranes;1988
3. Fluorescent probe studies on binding of glyceraldehyde-3-phosphate dehydrogenase to phosphatidylinositol liposomes Further evidence for conformational changes;FEBS Letters;1987-07-13
4. Supramolecular organization of glycolytic enzymes;Journal of Theoretical Biology;1985-10
5. Control of Enzyme Activity in Reversibly Adsorptive Enzyme Systems;Organized Multienzyme Systems: Catalytic Properties;1985
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