Dioscorin, the major tuber storage protein of yam (Dioscorea batatas Decne) with carbonic anhydrase and trypsin inhibitor activities

Wen Chi Hou, Jih Shiou Liu, Hsien Jung Chen, Tzeng Err Chen, Chung Fang Chang, Yaw Huei Lin

Research output: Contribution to journalArticle

73 Citations (Scopus)

Abstract

Dioscorin, the tuber storage protein of yam (Dioscorea batatas Decne), was purified successively by ammonium sulfate fractionation, DE-52 ion exchange chromatography, and Sephadex G-75 column. Two protein bands (82 and 28 kDa) were found under nonreducing conditions after SDS-PAGE; but only one band (32 kDa) was detected under reducing conditions. The first 21 amino acids in the N-terminal region of the 28 kDa form were VEDEFSYIEGNPNGPENWGNL, which was highly homologous to deductive sequence of dioscorin from cDNA of another yam species (Dioscorea cayenensis Lam) reported by Conlan et al. (Plant Mol. Biol. 1995, 28, 369-380). Hewett-Emmett and Tashian (Mol. Phylogenet. Evol. 1996, 5, 50-77) mentioned that, according to DNA alignments, dioscorin from yam (D. cayenensis) was α-carbonic anhydrase (α- CA) related. In this report, we found that the purified dioscorin showed both CA dehydration activity using sodium bicarbonate as a substrate and CA activity staining after SDS-PAGE. A polyclonal antibody, which was raised against trypsin inhibitor (TI), a storage protein of sweet potato (Ipomoea batatas [L.] Lam var. Tainong 57), cross-reacted with dioscorin, which also showed TI activity determined by both activity staining after SDS-PAGE and trypsin inhibition determination.

Original languageEnglish
Pages (from-to)2168-2172
Number of pages5
JournalJournal of Agricultural and Food Chemistry
Volume47
Issue number5
DOIs
Publication statusPublished - May 1999
Externally publishedYes

Fingerprint

Dioscorea polystachya
Dioscorea
Carbonic Anhydrase Inhibitors
Trypsin Inhibitors
yams
carbonate dehydratase
trypsin inhibitors
storage proteins
Dioscorea cayenensis
tubers
Ipomoea batatas
Polyacrylamide Gel Electrophoresis
Proteins
Sodium Bicarbonate
Carbonic Anhydrases
sodium bicarbonate
Ammonium Sulfate
ion exchange chromatography
sweet potatoes
Fractionation

Keywords

  • Carbonic anhydrase
  • Dioscorea batatas Decne
  • Dioscorin
  • Storage proteins
  • Trypsin inhibitor
  • Yam

ASJC Scopus subject areas

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

Cite this

Dioscorin, the major tuber storage protein of yam (Dioscorea batatas Decne) with carbonic anhydrase and trypsin inhibitor activities. / Hou, Wen Chi; Liu, Jih Shiou; Chen, Hsien Jung; Chen, Tzeng Err; Chang, Chung Fang; Lin, Yaw Huei.

In: Journal of Agricultural and Food Chemistry, Vol. 47, No. 5, 05.1999, p. 2168-2172.

Research output: Contribution to journalArticle

Hou, Wen Chi ; Liu, Jih Shiou ; Chen, Hsien Jung ; Chen, Tzeng Err ; Chang, Chung Fang ; Lin, Yaw Huei. / Dioscorin, the major tuber storage protein of yam (Dioscorea batatas Decne) with carbonic anhydrase and trypsin inhibitor activities. In: Journal of Agricultural and Food Chemistry. 1999 ; Vol. 47, No. 5. pp. 2168-2172.
@article{aeabb8fbd3bf4ea5830711a17d11fd19,
title = "Dioscorin, the major tuber storage protein of yam (Dioscorea batatas Decne) with carbonic anhydrase and trypsin inhibitor activities",
abstract = "Dioscorin, the tuber storage protein of yam (Dioscorea batatas Decne), was purified successively by ammonium sulfate fractionation, DE-52 ion exchange chromatography, and Sephadex G-75 column. Two protein bands (82 and 28 kDa) were found under nonreducing conditions after SDS-PAGE; but only one band (32 kDa) was detected under reducing conditions. The first 21 amino acids in the N-terminal region of the 28 kDa form were VEDEFSYIEGNPNGPENWGNL, which was highly homologous to deductive sequence of dioscorin from cDNA of another yam species (Dioscorea cayenensis Lam) reported by Conlan et al. (Plant Mol. Biol. 1995, 28, 369-380). Hewett-Emmett and Tashian (Mol. Phylogenet. Evol. 1996, 5, 50-77) mentioned that, according to DNA alignments, dioscorin from yam (D. cayenensis) was α-carbonic anhydrase (α- CA) related. In this report, we found that the purified dioscorin showed both CA dehydration activity using sodium bicarbonate as a substrate and CA activity staining after SDS-PAGE. A polyclonal antibody, which was raised against trypsin inhibitor (TI), a storage protein of sweet potato (Ipomoea batatas [L.] Lam var. Tainong 57), cross-reacted with dioscorin, which also showed TI activity determined by both activity staining after SDS-PAGE and trypsin inhibition determination.",
keywords = "Carbonic anhydrase, Dioscorea batatas Decne, Dioscorin, Storage proteins, Trypsin inhibitor, Yam",
author = "Hou, {Wen Chi} and Liu, {Jih Shiou} and Chen, {Hsien Jung} and Chen, {Tzeng Err} and Chang, {Chung Fang} and Lin, {Yaw Huei}",
year = "1999",
month = "5",
doi = "10.1021/jf980738o",
language = "English",
volume = "47",
pages = "2168--2172",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "5",

}

TY - JOUR

T1 - Dioscorin, the major tuber storage protein of yam (Dioscorea batatas Decne) with carbonic anhydrase and trypsin inhibitor activities

AU - Hou, Wen Chi

AU - Liu, Jih Shiou

AU - Chen, Hsien Jung

AU - Chen, Tzeng Err

AU - Chang, Chung Fang

AU - Lin, Yaw Huei

PY - 1999/5

Y1 - 1999/5

N2 - Dioscorin, the tuber storage protein of yam (Dioscorea batatas Decne), was purified successively by ammonium sulfate fractionation, DE-52 ion exchange chromatography, and Sephadex G-75 column. Two protein bands (82 and 28 kDa) were found under nonreducing conditions after SDS-PAGE; but only one band (32 kDa) was detected under reducing conditions. The first 21 amino acids in the N-terminal region of the 28 kDa form were VEDEFSYIEGNPNGPENWGNL, which was highly homologous to deductive sequence of dioscorin from cDNA of another yam species (Dioscorea cayenensis Lam) reported by Conlan et al. (Plant Mol. Biol. 1995, 28, 369-380). Hewett-Emmett and Tashian (Mol. Phylogenet. Evol. 1996, 5, 50-77) mentioned that, according to DNA alignments, dioscorin from yam (D. cayenensis) was α-carbonic anhydrase (α- CA) related. In this report, we found that the purified dioscorin showed both CA dehydration activity using sodium bicarbonate as a substrate and CA activity staining after SDS-PAGE. A polyclonal antibody, which was raised against trypsin inhibitor (TI), a storage protein of sweet potato (Ipomoea batatas [L.] Lam var. Tainong 57), cross-reacted with dioscorin, which also showed TI activity determined by both activity staining after SDS-PAGE and trypsin inhibition determination.

AB - Dioscorin, the tuber storage protein of yam (Dioscorea batatas Decne), was purified successively by ammonium sulfate fractionation, DE-52 ion exchange chromatography, and Sephadex G-75 column. Two protein bands (82 and 28 kDa) were found under nonreducing conditions after SDS-PAGE; but only one band (32 kDa) was detected under reducing conditions. The first 21 amino acids in the N-terminal region of the 28 kDa form were VEDEFSYIEGNPNGPENWGNL, which was highly homologous to deductive sequence of dioscorin from cDNA of another yam species (Dioscorea cayenensis Lam) reported by Conlan et al. (Plant Mol. Biol. 1995, 28, 369-380). Hewett-Emmett and Tashian (Mol. Phylogenet. Evol. 1996, 5, 50-77) mentioned that, according to DNA alignments, dioscorin from yam (D. cayenensis) was α-carbonic anhydrase (α- CA) related. In this report, we found that the purified dioscorin showed both CA dehydration activity using sodium bicarbonate as a substrate and CA activity staining after SDS-PAGE. A polyclonal antibody, which was raised against trypsin inhibitor (TI), a storage protein of sweet potato (Ipomoea batatas [L.] Lam var. Tainong 57), cross-reacted with dioscorin, which also showed TI activity determined by both activity staining after SDS-PAGE and trypsin inhibition determination.

KW - Carbonic anhydrase

KW - Dioscorea batatas Decne

KW - Dioscorin

KW - Storage proteins

KW - Trypsin inhibitor

KW - Yam

UR - http://www.scopus.com/inward/record.url?scp=0032841621&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032841621&partnerID=8YFLogxK

U2 - 10.1021/jf980738o

DO - 10.1021/jf980738o

M3 - Article

C2 - 10552514

AN - SCOPUS:0032841621

VL - 47

SP - 2168

EP - 2172

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 5

ER -