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All Journal HAYATI Journal of Biosciences Jurnal Kedokteran dan Kesehatan : Publikasi Ilmiah Fakultas Kedokteran Universitas Sriwijaya Global Medical and Health Communication Jurnal Sumberdaya Hayati Paediatrica Indonesiana Acta Biochimica Indonesiana Majalah Kedokteran Andalas Medika Kartika : Jurnal Kedokteran dan Kesehatan World Nutrition Journal Science Midwifery Jurnal Darma Agung JOURNAL LA MEDIHEALTICO Pharmaceutical And Biomedical Sciences Journal (PBSJ) Archives of Pediatric Gastroenterology, Hepatology, and Nutrition Molekul: Jurnal Ilmiah Kimia
Dwirini Retno Gunarti
Departemen Biokimia Dan Biologi Molekuler Fakultas Kedokteran Universitas Indonesia, Jl. Salemba Raya 6 Jakarta
Agriculture, Biological Sciences & Forestry Humanities Biochemistry, Genetics & Molecular Biology Chemistry Civil Engineering, Building, Construction & Architecture Computer Science & IT Decision Sciences, Operations Research & Management Dentistry Earth & Planetary Sciences Health Professions Immunology & microbiology Languange, Linguistic, Communication & Media Law, Crime, Criminology & Criminal Justice Library & Information Science Materials Science & Nanotechnology Medicine & Pharmacology Neuroscience Nursing Public Health Social Sciences Veterinary

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Journal : hayati journal of biosciences

 1 
Properties of Folate Binding Protein Purified from Cow’s Milk . SUBANDRATE; DWIRINI RETNO GUNARTI; MOHAMAD SADIKIN
HAYATI Journal of Biosciences Vol. 19 No. 3 (2012): September 2012
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (139.301 KB) | DOI: 10.4308/hjb.19.3.105

Abstract

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.
Isolation and Purification of Thiamine Binding Protein from Mung Bean GUNARTI, DWIRINI RETNO; RAHMI, HANIFAH; SADIKIN, MOHAMAD
HAYATI Journal of Biosciences Vol. 20 No. 1 (2013): March 2013
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (78.56 KB) | DOI: 10.4308/hjb.20.1.1

Abstract

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.
Co-Authors Agus Firmansyah Agus Firmansyah Andayani, Diyah Eka Annisa Rahmah Furqaani Asri Rasad Asri Rasad Badrya, Leily CHRIS ADHIYANTO Daldiyono Harjodisastro Ella Amalia, Ella Endi Ridwan Endi Ridwan Gantini, Ria Syafitri Evi HANIFAH RAHMI Hermansyah Hermansyah Hermansyah Katya Saphira Laifa Annisa Hendarmin Lusinanto, Arfat Mayasari, Citra Krisna Medina Athiah Mike Permata Sari Mohamad Sadikin MOHAMAD SADIKIN Mohamad Sadikin Mohamad Sadikin Muhammad Irsan Saleh Noor Diah Erlinawati Nugraha, Yudhi Nurul Ratna Mutu Manikam Octovia, Lily Indriani Rahmanita, Hania Asmarani Rustadi Sosrosumihardjo Rustadi Sosrosumihardjo Safyudin Saleh, Mgs. M. Irsan Samuel Oetoro Saputro, Alvreyna Cherienda Laviashna Septilia I. Wanandi Septilia Inawati Wanandi Sri Redjeki Subandrate Suri, Auliyani Andam Suwarsono, Erike A. Suwarsono A Wardani, Putri Kusuma Wulandari, Yohannessa Yudianita Kesuma, Yudianita Zen Hafy Zeti Harriyati