Spectral evidence for distinct mode of interaction of nucleotides with rabbit muscle and rabbit liver aldolase.
Ultraviolet difference spectra produced by the binding of mononucleotides and phosphates to rabbit aldolase A and B were analyzed. Both isozymes exhibit a distinct mode of interaction with the ligands. The binding seems to be based on multipoint interaction of nucleotides with each aldolase, indicating the existence of specific nucleotide binding domains in both proteins.
D000818:Animals; D005634:Fructose-Bisphosphate Aldolase; D007527:Isoenzymes; D008099:Liver / Q000201:enzymology; D046911:Macromolecular Substances; D009132:Muscles / Q000201:enzymology; D009711:Nucleotides; D011485:Protein Binding; D011817:Rabbits; D013056:Spectrophotometry, Ultraviolet
D007527:Isoenzymes; D046911:Macromolecular Substances; D009711:Nucleotides; D005634:Fructose-Bisphosphate Aldolase