Hostname: page-component-78c5997874-dh8gc Total loading time: 0 Render date: 2024-11-08T00:07:05.686Z Has data issue: false hasContentIssue false
  • English
  • Français

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
Get access Rights & Permissions [Opens in a new window]

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

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)