An approach based on diffusion to study ligand-macromolecule interaction.

Mohammad R Housaindokht; Mahmood Bahrololoom; Shirin Tarighatpoor; Ali A Mossavi-Movahedi

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PubMed · 12422240

An approach based on diffusion to study ligand-macromolecule interaction.

Mohammad R Housaindokht·Mahmood Bahrololoom·Shirin Tarighatpoor·Ali A Mossavi-Movahedi

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Abstract

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.

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Animals Azo Compounds Chickens Diffusion Egg Proteins Hydrogen-Ion Concentration Ligands Macromolecular Substances Models, Chemical Muramidase Protein Binding Spectrophotometry Temperature Journal Article

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Mohammad R Housaindokht, Mahmood Bahrololoom, Shirin Tarighatpoor, Ali A Mossavi-Movahedi. 2002. An approach based on diffusion to study ligand-macromolecule interaction.. https://pubmed.ncbi.nlm.nih.gov/12422240/

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