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Purification and properties of a highly active catalase from cabbage loopers, Trichoplusia ni

โœ Scribed by Martin J. Mitchell; Sami Ahmad; Ronald S. Pardini

Book ID
113168804
Publisher
Elsevier Science
Year
1991
Weight
568 KB
Volume
21
Category
Article
ISSN
0020-1790

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The majority of the JH Ill epoxide hydrolase activity in last stadium day 3 (gate 1) wandering Trichoplusia ni was membrane bound with approximately 9% of the activity found in the cytosol. Both the microsomal and cytosolic J H epoxide hydrolases were stable, retaining 30% of their original activity