Gels Mimicking Antibodies in Their Selective Recognition of Proteins and Its Potential Use for Protein Crystallization - Molecules: Nucleation, Aggregation and Crystallization - page 19

Fig. 4. Demonstration of the high degree of selective recognition of the adsorbent for
myoglobin from horse (M,h), myoglobin from whale (M,w), ribonuclease (R) and
cytochrome c (C). Analysis in a cation exchanger of (a) the fraction collected from a blank
column prepared in the absence of any protein, and (b) the fraction collected from a
column prepared in the presence of myoglobin from horse. A comparison of the two chro-
matogram traces shows that myoglobin from horse, but not that from whale, was adsorbed
onto the column prepared in the presence of the former protein, indicating a high degree
of selective recognition.
was low, which could be due to the smaller pore size of these gels with the
attendant difficulty of removing the protein to be specifically adsorbed.
Therefore, we studied another alternative for increasing the flow rate:
embedding grains of a soft gel with specific adsorption of a certain
protein into grains of a rigid gel (Hjertén et al ., 1997).