Taipei Medical University

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
Huang DJ
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------>journal_name=J. Agric. Food Chem.
------>paper_name=Active recombinant thioredoxin h protein with antioxidant activities from sweet potato (Ipomoea batatas L. Lam Tainong 57) storage roots
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------>fullAbstract=Recombinant thioredoxin h (Trx2) overproduced in Escherichia coli (M15) was purified by Ni2+-chelated affinity chromatography. The molecular mass of Trx2 is approximately 1.4 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Total antioxidant status, 1,1-diphenyl-2-picrylhydrazyl (DPPH) staining, reducing power method, Fe2+-chelating ability, ferric thiocyanate (FTC) method, and protection of calf thymus DNA against hydroxyl radical-induced damage were studied. The thioredoxin h protein with a concentration of 12.5 mg/mL exhibited the highest activity (expressed as 0.37 +/- 0.012 mM ABTS* radical cation being cleared) in a total antioxidant status test. In the DPPH staining thioredoxin h appeared as white spots when it was diluted to 50 mg/mL (a final amount of 15 microg). Like the total antioxidant status, the reducing power, Fe2+-chelating ability, FTC activity, and protection against hydroxyl radical-induced calf thymus DNA damage were found with the thioredoxin h protein. It was suggested that thioredoxin h might contribute to its antioxidant activities against hydroxyl and peroxyl radicals.
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------>authors2=Chen HJ
------>authors3=Hou WC
------>authors4=Lin CD
------>authors5=Lin YH
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------>authors=Huang DJ
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------>updateTitle=Active recombinant thioredoxin h protein with antioxidant activities from sweet potato (Ipomoea batatas [L.] Lam Tainong 57) storage roots.
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------>publish_year=2004
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A B C D E F G H I J K L M N O P Q R S T U V W X Y Z