Half-of-the-sites and all-of-the-sites reactivity in rabbit muscle glyceraldehyde 3-phosphate dehydrogenase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference21 articles.
1. Structure determination of crystalline lobster d-glyceraldehyde-3-phosphate dehydrogenase
2. Negative cooperativity in enzyme action. Binding of diphosphopyridine nucleotide to glyceraldehyde-3-phosphate dehydrogenase
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4. The isolation and specific activity of rabbit-muscle glyceraldehyde phosphate dehydrogenase
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2. Part-of-the-sites binding and reactivity in the homooligomeric enzymes – facts and artifacts;Archives of Biochemistry and Biophysics;2018-03
3. Expression, purification, enzymatic characterization and crystallization of glyceraldehyde-3-phosphate dehydrogenase from Naegleria gruberi , the first one from phylum Percolozoa;Protein Expression and Purification;2016-11
4. Quinone-induced inhibition of urease: Elucidation of its mechanisms by probing thiol groups of the enzyme;Bioorganic Chemistry;2007-06
5. Antibodies to inactive conformations of glyceraldehyde-3-phosphate dehydrogenase inactivate the apo-and holoforms of the enzyme;Biochemistry (Moscow);2006-06
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