Abstract
A new variety of affinity chromatography of enzymes is described which consists of building up an affinity adsorbent composed of a real substrate. The chromatography is performed at a sub-zero temperature where the turnover of the enzyme is very low or stopped. As a model system Sepharose-bound l-trialanine p-nitroanilide was for used the affinity binding of porcine pancreatic elastase, which was adsorbed to the column in a hypersaline medium at −14° and eluted from the column at the same temperature using 50% (v/v) ethylene glycol. The affinity adsorbent proved to be very specific as it did not retain trypsin, chymotrypsin and ovalbumin and retained only 20% of cytochrome c.
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