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Purification and immunochemical quantitation of Penicillium roqueforti acid aspartyl proteinase

Published online by Cambridge University Press:  01 February 1997

EMMANUELLE BRACQ ,
ANNIE LEVIEUX  and
DIDIER LEVIEUX
EMMANUELLE BRACQ
Affiliation:
Laboratoire de Recherches Fromagères, INRA, rue de Salers, F-15000 Aurillac, France
ANNIE LEVIEUX
Affiliation:
Unité d'Immunochimie, Station de Recherches sur la Viande, INRA, Theix, F-63122 Saint-Genès-Champanelle, France
DIDIER LEVIEUX
Affiliation:
Unité d'Immunochimie, Station de Recherches sur la Viande, INRA, Theix, F-63122 Saint-Genès-Champanelle, France
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Abstract

Acid aspartyl proteinase of Penicillium roqueforti was purified from culture filtrates using FPLC ion-exchange chromatography on Mono Q and size exclusion chromatography on Superdex 75. The purity obtained allowed us to produce, using rabbits, a specific antiserum which was then used to develop a sandwich ELISA. The test was sensitive (detection limit, 0·25 ng/ml), reproducible (CV, 3·1–6·9%) and closely correlated with enzyme activity measurement (r=0·995, P<0·001). This ELISA should be a valuable tool for monitoring acid aspartyl proteinase level in culture filtrates and for determining the enzyme activity[ratio ]enzyme protein ratio of acid aspartyl proteinase obtained after genetic recombinations or site-directed mutagenesis.

Type
Research Article
Information
Journal of Dairy Research , Volume 64 , Issue 1 , February 1997 , pp. 105 - 113
Copyright
Proprietors of Journal of Dairy Research 1997

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