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Restricted diffusion effect on the binding of proteins to porous polymer resins as studied by repetitive injection method
Author(s) -
Kitano Hiromi,
Nakamura Katsunori,
Hirai Youhei,
Kaku Takashi,
Ise Norio
Publication year - 1988
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260310606
Subject(s) - elution , bovine serum albumin , polymer , chromatography , chemistry , diffusion , porosity , serum albumin , packed bed , column (typography) , chemical engineering , organic chemistry , biochemistry , physics , structural engineering , connection (principal bundle) , engineering , thermodynamics
A solution of bovine serum albumin (BSA) is repeatedly injected into a column packed with highly porous and hydrophobic polymer resins at appropriate intervals. The injected BSA is thoroughly retained in the column for 10 injections and, afterwards, starts to be eluted from the column gradually. Taking into consideration the restricting effect of already bound BSA upon the diffusion of newly injected BSA into the pores of the polymer resins, we can interpret the BSA elution profile from columns packed with polymer resin of various pore sizes and porosities. The effects of the binding rate constant and BSA concentration upon the elution profiles of BSA are also analyzed. Formyl groups are introduced into the polymers as a binding site with proteins, and the elution profiles of BSA from the column packed with the formylated resin are also analyzed.