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Affinity precipitation of proteins by polyligands
Author(s) -
Morris John E.,
Hoffman Allan S.,
Fisher Rod R.
Publication year - 1993
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.260411010
Subject(s) - biotin , precipitation , chemistry , polyacrylamide , avidin , dissociation (chemistry) , ligand (biochemistry) , dissociation constant , chromatography , conjugated system , polymer , biochemistry , polymer chemistry , organic chemistry , receptor , physics , meteorology
A novel technique for affinity precipitation has been developed in which multimeric target proteins are precipitated as a result of network formation by polymer‐conjugated ligands (polyligands). A polyligand precipitant for avidin was synthesized by conjugation of biotin to a polyacrylamide‐based backbone. The effects of mixing conditions, ligand substitution frequency, and molecular weight on affinity precipitation were examined using the biotin‐PAAm precipitant. Biotin was replaced by iminobiotin to study the effect of the ligand‐protein dissociation constant o affinity precipitation. The iminobiotin‐PAAm precipitant was also used to examine the reversibility of the precipitation and recovery of the target protein after precipitation. © 1993 Wiley & Sons, Inc.