Association of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase. The biochemical and electron-microscopic evidence.
Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase covalently bound to Sepharose was shown to form a complex with soluble 3-phosphoglycerate kinase. The strength of the association appeared to depend upon the functional state of both enzymes. The holoform of the dehydrogenase exhibited a lower affinity for the kinase than the enzyme-3-phosphoglycerol.NADH complex. The substrate-free 3-phosphoglycerate kinase associated much stronger with the acylated dehydrogenase than the kinase in complex with 1,3-diphosphoglycerate. Electron-microscopic evidence for the association of the soluble acyl-glyceraldehyde-3-phosphate dehydrogenase.NADH complex and 3-phosphoglycerate kinase was also obtained.
Sukhodolets
M V
MV
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Muronetz
V I
VI
Tsuprun
V L
VL
Kaftanova
A S
AS
Nagradova
N K
NK
D000818:Animals; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D007700:Kinetics; D008854:Microscopy, Electron; D009097:Multienzyme Complexes / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology*; D010735:Phosphoglycerate Kinase / Q000378:metabolism*; D011817:Rabbits
D009097:Multienzyme Complexes; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D010735:Phosphoglycerate Kinase