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Isolation and Purification of Thiamine Binding Protein from Mung Bean

HAYATI Journal of Biosciences · Vol. 20 No. 1 (2013)

DOI
10.4308/hjb.20.1.1
ISSN
2086-4094, 1978-3019
Terbit
2013-03-28
Penerbit
Bogor Agricultural University, Indonesia
Bahasa
eng

Abstrak

Thiamine has fundamental role in energy metabolism. The organs mostly sensitive to the lack of thiamine levels in the body are the nervous system and the heart. Thiamine deficiency causes symptoms of polyneuritis and cardiovascular diseases. Because of its importance in the metabolism of carbohydrates, we need to measure the levels of thiamine in the body fluids by using an easy and inexpensive way without compromising the sensitivity and selectivity. An option to it is thiamine measurement based on the principle of which is analogous to ELISA, in which a thiamine binding protein (TBP) act by replacing antibodies. The presence of TBP in several seeds have been reported by previous researchers, but the presence of TBP in mung beans has not been studied. This study was aimed to isolate and purify TBP from mung bean. The protein was isolated from mung bean through salting out by ammonium sulphate of 40, 70, and 90% (w/v). TBP has a negative charge as shown by cellulose acetate electrophoresis. The result obtained after salting out by ammonium sulphate was further purified bymeans of DEAE-cellulose chromatography and affinity chromatography. In precipitation of 90% of salting out method, one peak protein was obtained by using affinity chromatography. The protein was analyzed by SDS PAGE electrophoresis. The result of SDS PAGE electrophoresis showed that TBP has a molecular weight of 72.63 kDa.

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  • University of Indonesia
  • Universitas Muhammadiyah Prof Dr Hamka
  • Sriwijaya University
  • National Nuclear Energy Agency of Indonesia
  • State University of Jakarta
  • University of Liverpool
  • National Research and Innovation Agency
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Rekan penulisOrganisasiArtikel bersama
Rini PuspitaningrumState University of Jakarta4
Septelia Inawati WanandiUniversity of Indonesia3
RONDANG ROEMIATI SOEGIANTOUniversitas Kristen Indonesia3
Wawan MulyawanUniversity of Indonesia2
Sri Widia A. JusmanUniversity of Indonesia2
. SUBANDRATEAfiliasi tidak diketahui2
Mgs. M. Irsan SalehSriwijaya University2
Subandrate SubandrateSriwijaya University2
Hermansyah HermansyahSriwijaya University2
Zen HafySriwijaya University2
Yudianita KesumaSriwijaya University2
Siska SiskaUniversitas Muhammadiyah Prof Dr Hamka1
Almawati SitumorangUniversitas Muhammadiyah Prof Dr Hamka1
I. LestariUniversity of Indonesia1
Dian Pribadi PerkasaNational Nuclear Energy Agency of Indonesia1
Hariyanti HariyantiUniversitas Muhammadiyah Prof Dr Hamka1
E ErizalNational Nuclear Energy Agency of Indonesia1
Rizal ApriyaniUniversitas Muhammadiyah Prof Dr Hamka1
Iin KurniaNational Nuclear Energy Agency of Indonesia1
Teja KisnantoNational Nuclear Energy Agency of Indonesia1
DARYL ROBERT WILLIAMSUniversity of Liverpool1
Andrew R. CossinsUniversity of Liverpool1
RusdiAfiliasi tidak diketahui1
Kurnia Nuztir MantoliniState University of Jakarta1
Wahono SumaryonoBadan Pengkajian dan Penerapan Teknologi1
Amarila MalikUniversity of Indonesia1
Trismilah MargonoUniversity of Indonesia1
Margaretha HerawatiUniversitas Prof Dr Moestopo1
WardayaAfiliasi tidak diketahui1
Fanny Septiani FarhanUniversitas Muhammadiyah Jakarta1
Frans FerdinalTarumanagara University1
Wardaya WardayaUniversity of Indonesia1
Fitrine EkawastiNational Research and Innovation Agency1
April Hari WardhanaNational Research and Innovation Agency1
Dyah Haryuningtyas SawitriAfiliasi tidak diketahui1
Heri WibowoUniversity of Indonesia1

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Sumber metadata: OAI-PMH (metadata jurnal) http://journal.ipb.ac.id/index.php/hayati/oai, pertama di-harvest 8 Nov 2026, terakhir terlihat 8 Nov 2026.
Metadata asli (oai_dc)
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	<dc:title xml:lang="en">Isolation and Purification of Thiamine Binding Protein from Mung Bean</dc:title>
	<dc:creator xml:lang="en">GUNARTI, DWIRINI RETNO</dc:creator>
	<dc:creator xml:lang="en">RAHMI, HANIFAH</dc:creator>
	<dc:creator xml:lang="en">SADIKIN, MOHAMAD</dc:creator>
	<dc:subject xml:lang="en">chromatography</dc:subject>
	<dc:subject xml:lang="en">electrophoresis</dc:subject>
	<dc:subject xml:lang="en">mung bean</dc:subject>
	<dc:subject xml:lang="en">thiamine</dc:subject>
	<dc:subject xml:lang="en">thiamine binding protein</dc:subject>
	<dc:description xml:lang="en">Thiamine has fundamental role in energy metabolism. The organs mostly sensitive to the lack of thiamine levels in the body are the nervous system and the heart. Thiamine deficiency causes symptoms of polyneuritis and cardiovascular diseases. Because of its importance in the metabolism of carbohydrates, we need to measure the levels of thiamine in the body fluids by using an easy and inexpensive way without compromising the sensitivity and selectivity. An option to it is thiamine measurement based on the principle of which is analogous to ELISA, in which a thiamine binding protein (TBP) act by replacing antibodies. The presence of TBP in several seeds have been reported by previous researchers, but the presence of TBP in mung beans has not been studied. This study was aimed to isolate and purify TBP from mung bean. The protein was isolated from mung bean  through salting out by ammonium sulphate of 40, 70, and 90% (w/v). TBP has a negative charge as shown by cellulose acetate electrophoresis. The result obtained after salting out by ammonium sulphate was further purified bymeans of DEAE-cellulose chromatography and affinity chromatography. In precipitation of 90% of salting out method, one peak protein was obtained by using affinity chromatography. The protein was analyzed by SDS PAGE electrophoresis. The result of SDS PAGE electrophoresis showed that TBP has a molecular weight of 72.63 kDa.</dc:description>
	<dc:publisher xml:lang="en">Bogor Agricultural University, Indonesia</dc:publisher>
	<dc:date>2013-03-28</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
	<dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
	<dc:type xml:lang="en">Peer-reviewed Article</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>http://journal.ipb.ac.id/hayati/article/view/6639</dc:identifier>
	<dc:identifier>10.4308/hjb.20.1.1</dc:identifier>
	<dc:source xml:lang="en">HAYATI Journal of Biosciences; Vol. 20 No. 1 (2013): March 2013; 1</dc:source>
	<dc:source>2086-4094</dc:source>
	<dc:source>1978-3019</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>http://journal.ipb.ac.id/hayati/article/view/6639/6639</dc:relation>
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