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Properties of Folate Binding Protein Purified from Cow’s Milk

HAYATI Journal of Biosciences · Vol. 19 No. 3 (2012)

DOI
10.4308/hjb.19.3.105
ISSN
2086-4094, 1978-3019
Terbit
2012-10-15
Penerbit
Bogor Agricultural University, Indonesia
Bahasa
eng

Abstrak

Folic acid played an important role in the metabolism of the body. To measure the serum folic acid levels could use the folate binding protein (FBP) from cow’s milk with a technique analogous to ELISA. The aims of this study were to identify characteristics of FBP from cow’s milk and binding capacity of FBP to folic acid and to purify FBP from other whey protein passed through DEAE-cellulose chromatography column. Each of DEAE-cellulose peaks was passed in affinity chromatography column. FBP was released from affinity column with sodium acetate buffer pH 3.5. The purity of obtained FBP was demonstrated by a single spot in SDS-PAGE analysis and the estimated molecular weight of FBP was around 31 kDa. Our study indicated that 1 mol FBP bound 1 mol folic acid. Alkylation with iodoacetic acid decreased the binding capacity of FBP which suggested the presence of a–SH or imidazol group in its active site. The importance of disulfide bridge was proven by decreasing of folate binding capacity of FBP after b-mercaptoethanol treatment. In contrary, the folate binding didn need Ca2+ ion, as indicated by EDTA test which gave the same result as control.

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  • University of Indonesia
  • Sriwijaya University
  • State University of Jakarta
  • National Nuclear Energy Agency of Indonesia
  • University of Liverpool
  • National Research and Innovation Agency
  • Universitas Kristen Indonesia
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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
Hanifah RahmiUniversitas Muhammadiyah Prof Dr Hamka2
Mgs. M. Irsan SalehSriwijaya University2
Subandrate SubandrateSriwijaya University2
Hermansyah HermansyahSriwijaya University2
Zen HafySriwijaya University2
Yudianita KesumaSriwijaya University2
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">Properties of Folate Binding Protein Purified from Cow’s Milk</dc:title>
	<dc:creator xml:lang="en">SUBANDRATE, .</dc:creator>
	<dc:creator xml:lang="en">GUNARTI, DWIRINI RETNO</dc:creator>
	<dc:creator xml:lang="en">SADIKIN, MOHAMAD</dc:creator>
	<dc:subject xml:lang="en">folate binding protein</dc:subject>
	<dc:subject xml:lang="en">folic acid</dc:subject>
	<dc:subject xml:lang="en">binding capacity</dc:subject>
	<dc:description xml:lang="en">Folic acid played an important role in the metabolism of the body. To measure the serum folic acid levels could use the folate binding protein (FBP) from cow’s milk with a technique analogous to ELISA.  The aims of this study were to identify characteristics of FBP from cow’s milk and binding capacity of FBP to folic acid and to purify FBP from other whey protein passed through DEAE-cellulose chromatography column. Each of DEAE-cellulose peaks was passed in affinity chromatography column. FBP was released from affinity column with sodium acetate buffer pH 3.5. The purity of obtained FBP was demonstrated by a single spot in SDS-PAGE analysis and the estimated molecular weight of FBP was around 31 kDa. Our study indicated that 1 mol FBP bound 1 mol folic acid. Alkylation with iodoacetic acid decreased the binding capacity of FBP which suggested the presence of a–SH or imidazol group in its active site. The importance of disulfide bridge was proven by decreasing of folate binding capacity of FBP after b-mercaptoethanol treatment. In contrary, the folate binding didn need Ca2+ ion, as indicated by EDTA test which gave the same result as control.</dc:description>
	<dc:publisher xml:lang="en">Bogor Agricultural University, Indonesia</dc:publisher>
	<dc:date>2012-10-15</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/5621</dc:identifier>
	<dc:identifier>10.4308/hjb.19.3.105</dc:identifier>
	<dc:source xml:lang="en">HAYATI Journal of Biosciences; Vol. 19 No. 3 (2012): September 2012; 105</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/5621/4265</dc:relation>
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