Active recombinant thioredoxin h protein with antioxidant activities from sweet potato (Ipomoea batatas [L.] Lam Tainong 57) storage roots

Dong Jiann Huang, Hsien Jung Chen, Wen Chi Hou, Chun Der Lin, Yaw Huei Lin

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Recombinant thioredoxin h (Trx2) overproduced in Escherichia colI (M 15) was purified by Ni2+-chelated affinity chromatography. The molecular mass of Trx2 is ∼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, Fe 2+-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 μg). 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.

Original languageEnglish
Pages (from-to)4720-4724
Number of pages5
JournalJournal of Agricultural and Food Chemistry
Volume52
Issue number15
DOIs
Publication statusPublished - Jul 28 2004

Fingerprint

Thioredoxin h
Ipomoea batatas
sweet potatoes
thiocyanates
Antioxidants
antioxidant activity
hydroxyl radicals
antioxidants
Hydroxyl Radical
calves
Chelation
Proteins
proteins
affinity chromatography
DNA damage
biphenyl
polyacrylamide gel electrophoresis
cations
Staining and Labeling
Affinity chromatography

Keywords

  • Antioxidant
  • CDNA sequence
  • Gene expression
  • Recombinant protein
  • Sweet potato
  • Thioredoxin h

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Food Science
  • Chemistry (miscellaneous)

Cite this

Active recombinant thioredoxin h protein with antioxidant activities from sweet potato (Ipomoea batatas [L.] Lam Tainong 57) storage roots. / Huang, Dong Jiann; Chen, Hsien Jung; Hou, Wen Chi; Lin, Chun Der; Lin, Yaw Huei.

In: Journal of Agricultural and Food Chemistry, Vol. 52, No. 15, 28.07.2004, p. 4720-4724.

Research output: Contribution to journalArticle

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abstract = "Recombinant thioredoxin h (Trx2) overproduced in Escherichia colI (M 15) was purified by Ni2+-chelated affinity chromatography. The molecular mass of Trx2 is ∼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, Fe 2+-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 μg). 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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