Fluorescence investigations on the interaction of rabbit liver D-fructose-1,6-bisphosphate 1-phosphohydrolase with bovine serum albumin.
The interaction of D-fructose-1,6-bisphosphate 1-phosphohydrolase (Fru-P2-ase, EC 3.1.3.11), with bovine serum albumin (BSA) results in the fluorescence quenching of BSA. BSA increases fluorescence anisotropy of Fru-P2-ase modified with o-phthaldialdehyde. A program in Fortran, to simulate the experimental titration curves of BSA with Fru-P2-ase and o-phthaldialdehyde modified Fru-P2-ase with BSA, was written. For fluorescence quenching experiments the best fit was obtained for a model where one subunit of native Fru-P2-ase binds up two molecules of BSA. The determined dissociation constants at 5, 15, 25 and 35 degrees C were 2.2, 1.6, 0.83 and 0.03 microM, respectively.
Dzugaj
A
A
Department of Animal Physiology, University of Wrocław, Poland.
Gancarz
R
R
D000818:Animals; D005454:Fluorescence Polarization; D007700:Kinetics; D008099:Liver / Q000201:enzymology / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism; D011199:Potentiometry; D011817:Rabbits; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence / Q000379:methods; D009764:o-Phthalaldehyde / Q000032:analysis / Q000737:chemistry
D012710:Serum Albumin, Bovine; D009764:o-Phthalaldehyde; D010447:Peptide Hydrolases; C020152:fructose 1,6-bisphosphatase converting enzyme