AFFINITY CHROMATOGRAPHY AT SUB-ZERO TEMPERATURES - MODEL STUDY WITH PORCINE PANCREATIC ELASTASE

被引:11
作者
BALNY, C [1 ]
LEDOUCEN, C [1 ]
DOUZOU, P [1 ]
BIETH, JG [1 ]
机构
[1] UNIV LOUIS PASTEUR,ENZYMOL LAB,F-67083 STRASBOURG,FRANCE
来源
JOURNAL OF CHROMATOGRAPHY | 1979年 / 168卷 / 01期
关键词
D O I
10.1016/S0021-9673(00)80701-3
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
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. © 1979.
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页码:133 / 138
页数:6
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