Evidence for a change in catalytic properties of glyceraldehyde 3-phosphate dehydrogenase monomers upon their association in a tetramer
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(82)80565-6/fullpdf
Reference15 articles.
1. Half-of-the-sites reactivity in immobilized hybrids of glyceraldehyde-3-phosphate dehydrogenase
2. Immobilized d-glyceraldehyde-3-phosphate dehydrogenase can exist as a trimer
3. Half-of-the-sites reactivity of yeast glyceraldehyde 3-phosphate dehydrogenase
4. Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase
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1. Coimmobilization of lactate dehydrogenase and low-molecular-weight thiols on sepharose;Applied Biochemistry and Microbiology;2001
2. Antibodies to the Nonnative Forms of d-Glyceraldehyde-3-Phosphate Dehydrogenase: Identification, Purification, and Influence on the Renaturation of the Enzyme;Archives of Biochemistry and Biophysics;1999-09
3. Study on the interactions between protein disulfide isomerase and target proteins, using immobilization on solid support;FEBS Letters;1998-04-10
4. Glyceraldehyde-3-phosphate dehydrogenase;Enzyme Handbook;1993
5. Calculation of the free energy of association for protein complexes;Protein Science;1992-01
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