Open AccessPhysico‐chemical Evidence for the Interaction between Aldolase and Glyceraldehyde‐3‐phosphate Dehydrogenase
Author(s) -
OVÁDI Judit,
KELETI Tamás,
SALERNO Costantino,
FASELLA Paolo
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12629.x
Subject(s) - aldolase a , glyceraldehyde , dehydrogenase , glyceraldehyde 3 phosphate dehydrogenase , tetramer , fructose bisphosphate aldolase , aldolase b , biochemistry , chemistry , dissociation constant , dissociation (chemistry) , enzyme , organic chemistry , receptor
Polarization of fluorescence measurements of aldolase and d ‐glyceraldehyde‐3‐phosphate dehydrogenase labeled with fluorescein isothiocyanate have been used to detect the possible formation of a soluble complex between the proteins. The results suggest an interaction between aldolase and d ‐glyceraldehyde‐3‐phosphate dehydrogenase with an apparent dissociation constant 3 × 10 −7 M and an apparent stoichiometry of two aldolase tetramers bound per tetramer of d ‐glyceraldehyde‐3‐phosphate dehydrogenase.