A complex containing both trypsin inhibitor and dehydroascorbate reductase activities isolated from mitochondria of etiolated mung bean (Vigna radiata L. (Wilczek) cv. Tainan No. 5) seedlings

Wen C. Hou, Yuh T. Wang, Yaw Huei Lin, Lin June Hsiao, Tzeng E. Chen, Chiu W. Wang, Hwa Dai

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

A complex containing trypsin inhibitor (TI) activity was extracted with 0.1 M TRIS buffer (pH 7.9) from trypsin-treated mitochondria of etiolated mung bean seedlings, and further purified with a Superdex 200 FPLC column. This partially purified complex with an Mr about 820 kDa exhibited additional dehydroascorbate (DHA) reductase activity with specific activities of 0.21, 1.53 and 1.54 μmol ascorbate formed min-1 mg-1 protein at pH 6.0, 6.5 and 7.0, respectively, when glutathione was added. Much lower DHA reductase activity (0.013 and 0.026 μmol ascorbate formed min-1 mg-1 protein at pH 6.5 and 7.0, respectively) was found when glutathione was omitted. The isolated complex gave positive results when it was tested by TI activity staining after SDS-PAGE, and could be recognized by a polyclonal antibody which was raised against 38 kDa sweet potato Kunitz-type TI, one of the root storage proteins of sweet potato. The possible physiological functions of this complex with both TI and DHA reductase activities were discussed.

Original languageEnglish
Pages (from-to)713-719
Number of pages7
JournalJournal of Experimental Botany
Volume51
Issue number345
Publication statusPublished - Apr 2000
Externally publishedYes

Fingerprint

glutathione dehydrogenase (ascorbate)
Trypsin Inhibitors
Vigna radiata
trypsin inhibitors
mung beans
Seedlings
Mitochondria
mitochondria
sweet potatoes
Ipomoea batatas
seedlings
glutathione
Kunitz-type proteinase inhibitor
Glutathione
storage proteins
polyclonal antibodies
trypsin
Proteins
buffers
proteins

Keywords

  • Dehydroascorbate reductase
  • Glutathione
  • Mitochondria
  • Mung bean
  • Sweet potato
  • Trypsin inhibitor

ASJC Scopus subject areas

  • Plant Science

Cite this

A complex containing both trypsin inhibitor and dehydroascorbate reductase activities isolated from mitochondria of etiolated mung bean (Vigna radiata L. (Wilczek) cv. Tainan No. 5) seedlings. / Hou, Wen C.; Wang, Yuh T.; Lin, Yaw Huei; Hsiao, Lin June; Chen, Tzeng E.; Wang, Chiu W.; Dai, Hwa.

In: Journal of Experimental Botany, Vol. 51, No. 345, 04.2000, p. 713-719.

Research output: Contribution to journalArticle

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abstract = "A complex containing trypsin inhibitor (TI) activity was extracted with 0.1 M TRIS buffer (pH 7.9) from trypsin-treated mitochondria of etiolated mung bean seedlings, and further purified with a Superdex 200 FPLC column. This partially purified complex with an Mr about 820 kDa exhibited additional dehydroascorbate (DHA) reductase activity with specific activities of 0.21, 1.53 and 1.54 μmol ascorbate formed min-1 mg-1 protein at pH 6.0, 6.5 and 7.0, respectively, when glutathione was added. Much lower DHA reductase activity (0.013 and 0.026 μmol ascorbate formed min-1 mg-1 protein at pH 6.5 and 7.0, respectively) was found when glutathione was omitted. The isolated complex gave positive results when it was tested by TI activity staining after SDS-PAGE, and could be recognized by a polyclonal antibody which was raised against 38 kDa sweet potato Kunitz-type TI, one of the root storage proteins of sweet potato. The possible physiological functions of this complex with both TI and DHA reductase activities were discussed.",
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T1 - A complex containing both trypsin inhibitor and dehydroascorbate reductase activities isolated from mitochondria of etiolated mung bean (Vigna radiata L. (Wilczek) cv. Tainan No. 5) seedlings

AU - Hou, Wen C.

AU - Wang, Yuh T.

AU - Lin, Yaw Huei

AU - Hsiao, Lin June

AU - Chen, Tzeng E.

AU - Wang, Chiu W.

AU - Dai, Hwa

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N2 - A complex containing trypsin inhibitor (TI) activity was extracted with 0.1 M TRIS buffer (pH 7.9) from trypsin-treated mitochondria of etiolated mung bean seedlings, and further purified with a Superdex 200 FPLC column. This partially purified complex with an Mr about 820 kDa exhibited additional dehydroascorbate (DHA) reductase activity with specific activities of 0.21, 1.53 and 1.54 μmol ascorbate formed min-1 mg-1 protein at pH 6.0, 6.5 and 7.0, respectively, when glutathione was added. Much lower DHA reductase activity (0.013 and 0.026 μmol ascorbate formed min-1 mg-1 protein at pH 6.5 and 7.0, respectively) was found when glutathione was omitted. The isolated complex gave positive results when it was tested by TI activity staining after SDS-PAGE, and could be recognized by a polyclonal antibody which was raised against 38 kDa sweet potato Kunitz-type TI, one of the root storage proteins of sweet potato. The possible physiological functions of this complex with both TI and DHA reductase activities were discussed.

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