Dehydroascorbate reductase and monodehydroascorbate reductase activities of trypsin inhibitors, the major sweet potato (Ipomoea batatas [L.] Lam) root storage protein

Wen C. Hou, Yaw Huei Lin

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

Trypsin inhibitors (TIs) were purified from the storage roots of sweet potato (Ipomoea batatas [L.] Lam var. Tainong 57) with ammonium sulfate precipitation, Sephadex G-75 gel filtration chromatography, and trypsin- Sepharose 4B affinity chromatography as previously reported [1]. Dehydroascorbate (DHA) was reduced by TIs independent of glutathione to regenerate ascorbate (AsA) contrasting with the function of DHA reductase with glutathione as a cofactor. Intermolecular thiol-disulfide interchanges of TIs were found during DHA reduction. AsA was oxidized by AsA oxidase to generate monodehydroascorbate (MDA) free radicals. MDA was reduced also by TIs to AsA in the presence of NADH which was the function of MDA reductase. The physiological significance of TIs with both DHA reductase and MDA reductase activities are discussed.

Original languageEnglish
Pages (from-to)151-158
Number of pages8
JournalPlant Science
Volume128
Issue number2
DOIs
Publication statusPublished - Oct 13 1997
Externally publishedYes

Fingerprint

glutathione dehydrogenase (ascorbate)
Ipomoea batatas
monodehydroascorbate reductase (NADH)
Trypsin Inhibitors
trypsin inhibitors
storage proteins
sweet potatoes
Oxidoreductases
Proteins
Glutathione
glutathione
Ascorbate Oxidase
ascorbate oxidase
Affinity chromatography
Ammonium Sulfate
Interchanges
affinity chromatography
Chromatography
thiols
Affinity Chromatography

Keywords

  • Dehydroascorbate
  • DHA reductase
  • Ipomoea batatas (L.) Lam
  • MDA reductase
  • Monodehydroascorbate
  • Trypsin inhibitor

ASJC Scopus subject areas

  • Plant Science
  • Biochemistry
  • Biotechnology

Cite this

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title = "Dehydroascorbate reductase and monodehydroascorbate reductase activities of trypsin inhibitors, the major sweet potato (Ipomoea batatas [L.] Lam) root storage protein",
abstract = "Trypsin inhibitors (TIs) were purified from the storage roots of sweet potato (Ipomoea batatas [L.] Lam var. Tainong 57) with ammonium sulfate precipitation, Sephadex G-75 gel filtration chromatography, and trypsin- Sepharose 4B affinity chromatography as previously reported [1]. Dehydroascorbate (DHA) was reduced by TIs independent of glutathione to regenerate ascorbate (AsA) contrasting with the function of DHA reductase with glutathione as a cofactor. Intermolecular thiol-disulfide interchanges of TIs were found during DHA reduction. AsA was oxidized by AsA oxidase to generate monodehydroascorbate (MDA) free radicals. MDA was reduced also by TIs to AsA in the presence of NADH which was the function of MDA reductase. The physiological significance of TIs with both DHA reductase and MDA reductase activities are discussed.",
keywords = "Dehydroascorbate, DHA reductase, Ipomoea batatas (L.) Lam, MDA reductase, Monodehydroascorbate, Trypsin inhibitor",
author = "Hou, {Wen C.} and Lin, {Yaw Huei}",
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T1 - Dehydroascorbate reductase and monodehydroascorbate reductase activities of trypsin inhibitors, the major sweet potato (Ipomoea batatas [L.] Lam) root storage protein

AU - Hou, Wen C.

AU - Lin, Yaw Huei

PY - 1997/10/13

Y1 - 1997/10/13

N2 - Trypsin inhibitors (TIs) were purified from the storage roots of sweet potato (Ipomoea batatas [L.] Lam var. Tainong 57) with ammonium sulfate precipitation, Sephadex G-75 gel filtration chromatography, and trypsin- Sepharose 4B affinity chromatography as previously reported [1]. Dehydroascorbate (DHA) was reduced by TIs independent of glutathione to regenerate ascorbate (AsA) contrasting with the function of DHA reductase with glutathione as a cofactor. Intermolecular thiol-disulfide interchanges of TIs were found during DHA reduction. AsA was oxidized by AsA oxidase to generate monodehydroascorbate (MDA) free radicals. MDA was reduced also by TIs to AsA in the presence of NADH which was the function of MDA reductase. The physiological significance of TIs with both DHA reductase and MDA reductase activities are discussed.

AB - Trypsin inhibitors (TIs) were purified from the storage roots of sweet potato (Ipomoea batatas [L.] Lam var. Tainong 57) with ammonium sulfate precipitation, Sephadex G-75 gel filtration chromatography, and trypsin- Sepharose 4B affinity chromatography as previously reported [1]. Dehydroascorbate (DHA) was reduced by TIs independent of glutathione to regenerate ascorbate (AsA) contrasting with the function of DHA reductase with glutathione as a cofactor. Intermolecular thiol-disulfide interchanges of TIs were found during DHA reduction. AsA was oxidized by AsA oxidase to generate monodehydroascorbate (MDA) free radicals. MDA was reduced also by TIs to AsA in the presence of NADH which was the function of MDA reductase. The physiological significance of TIs with both DHA reductase and MDA reductase activities are discussed.

KW - Dehydroascorbate

KW - DHA reductase

KW - Ipomoea batatas (L.) Lam

KW - MDA reductase

KW - Monodehydroascorbate

KW - Trypsin inhibitor

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