An approach based on diffusion to study ligand-macromolecule interaction.
A new approach has been developed to study binding of a ligand to a macromolecule based on the diffusion process. In terms of the Fick's first law, the concentration of free ligand in the presence of a protein can be determined by the measurement of those ligands which are diffused out. This method is applied to the study of binding of methyl-orange to lysozyme in phosphate buffer of pH 6.2, at 30 degrees C. The binding isotherm was determined initially, followed by application of the Hill equation to the data obtained, then binding constant and binding capacity were estimated.
Housaindokht
Mohammad R
MR
Department of Chemistry, Faculty of Science, Ferdowsi University of Mashhad, Iran. Mhousaindokht@science1.um.ac.ir
Bahrololoom
Mahmood
M
Tarighatpoor
Shirin
S
Mossavi-Movahedi
Ali A
AA
D000818:Animals; D001391:Azo Compounds / Q000378:metabolism*; D002645:Chickens; D004058:Diffusion; D004527:Egg Proteins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D046911:Macromolecular Substances; D008956:Models, Chemical; D009113:Muramidase / Q000378:metabolism*; D011485:Protein Binding; D013053:Spectrophotometry / Q000379:methods; D013696:Temperature
D001391:Azo Compounds; D004527:Egg Proteins; D008024:Ligands; D046911:Macromolecular Substances; C100258:methyl orange; D009113:Muramidase