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Affinity chromatography at sub-zero temperatures. A model study with porcine pancreatic elastase.

C Balny·C Le Doucen·P Douzou·J G Bieth
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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 degrees and eluted from the column at the same temperature using 50% (v/v) ethylene glycol. The affinity adsorbent proved to be vary specific as it did not retain trypsin, chymotrypsin and ovalbumin and retained only 20% of cytochrome c.

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AnimalsChromatography, AffinityFreezingIn Vitro TechniquesKineticsPancreasPancreatic ElastaseSwineJournal Article

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C Balny, C Le Doucen, P Douzou, J G Bieth. 1979-01-11. Affinity chromatography at sub-zero temperatures. A model study with porcine pancreatic elastase.. https://doi.org/10.1016/s0021-9673(00)80701-3

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