Dynamic Dialysis Utilizing a Hollow Fibre Unit as a Rapid Method for Studying Protein Bindings

Abstract

A useful approach for determining the binding ability which occurres in a protein-small molecule system was studied by a method of dynamic dialysis utilizing a hollow fibre unit. A dependency on experimental variables in the absence of protein was examined in order to characterize the nature of the dialytic process. It was shown that the rate of small molecule escaped across the dialytic membrane was dependent on stirring or flowing rate, temperature and pH, but independent on buffer strength or viscosity. The protein binding ability was examined by means of comparing amounts of small molecules in the absence and presence of protein. Kinetic parameters for the binding behaviour analysed from the Scatchard plot in the present experiment were in agreement with values previously reported.

Tobramycin Disposition in the Rat Lung Following Airway Administration

“…In the current study, the dynamic dialysis techniques, first described by Meyer and Guttman and used subsequently by other groups to study solute-ligand binding (Meyer andGuttman, 1968, 1970;Bottari et al, 1975;Pedersen et al, 1977;Hiji et al, 1978;Sparrow et al, 1982;Hashimoto et al, 1984), were first used to support the use of the IPRL binding and sequestration model described in Scheme 2. When dynamic dialysis under sink conditions is used to extract solutes from sliced IPRL tissue following initial airway dosing to that tissue, a model analogous to Scheme 2, Scheme 3 applies (Meyer and Guttman, 1968).…”