Gels Mimicking Antibodies in Their Selective Recognition of Proteins and Its Potential Use for Protein Crystallization - Molecules: Nucleation, Aggregation and Crystallization - page 30

enzyme will be adsorbed. The “enzyme reactors” can also be used as the
screening element in biosensors (Hjertén et al ., 2008)
The design of a chromatographic bed for
removal of impurifying proteins
(“negative purification”)
The impurifying proteins can be found for instance in the mother liquor
(crystallization cocktail) at crystallization and in the supernatant at pre-
cipitation. Artificial gel antibodies against the proteins can easily be pre-
pared by the addition of acrylamide and bis-acrylamide to these solutions.
Following polymerization the gel formed is granulated and the proteins
are removed (see, Section “Preparation of a ribonuclease specific gel”).
Forthcoming studies
The mechanism of selective recognition is only one of many questions
which importunately insist upon an answer. Others are: How does one
elute the protein adsorbed specifically in a small volume and in a gentle
way? Does a high selectivity require a high rigidity of the solute; if so,
should the solute molecules be cross-linked (reversibly)? Analogous elec-
trophoretic methods should also be developed, and the studies of methods
based on “negative purification” should be intensified and employed in
experiments aimed at crystallization of proteins.
Conclusions
The experiments described in this paper strengthen the hypothesis that it
is possible to design gels which resemble chemically and biologically
antibodies in the sense that they recognize selectively and bind strongly
a particular protein, virus or bacterium (and other bioparticles). A prereq-
uisite seems to be that the number of bonds between the gel and the antigen
is large and that each bond is relatively weak. The ease and simplicity by