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MOHAMAD SADIKIN
Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Indonesia
Agriculture, Biological Sciences & Forestry Earth & Planetary Sciences

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Isolation and Purification of Thiamine Binding Protein from Mung Bean DWIRINI RETNO GUNARTI; HANIFAH RAHMI; MOHAMAD SADIKIN
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.
Comparison of Hemoglobins from Various Subjects Living in Hypoxia RINI PUSPITANINGRUM; KURNIA NUZTIR MANTOLINI; . RUSDI; MOHAMAD SADIKIN
HAYATI Journal of Biosciences Vol. 20 No. 3 (2013): September 2013
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (78.296 KB) | DOI: 10.4308/hjb.20.3.99

Abstract

The aim of this research was to obtain the different characteristics of haemoglobin molecules in subjects under hypoxic condition, namely eel, catfish, suckermouth fish, green sea turtle using an electrophoresis technique. We used human umbilical cord blood and thalassemia patient blood, as well as a normal adult-human blood as controls. The proteins obtained after electrophoresis process were stained with two different colouring techniques, each based on different principles. Both staining techniques gave practically identical results. Subject that live in hypoxic condition has a different haemoglobin in comparison to the one found in adult human live in normal oxygen condition (normoxia). These hypoxia-adapted or -needed hemoglobin migrate slower than adult human hemoglobin from normoxia. This observation suggests that hemoglobin which is needed to live in hypoxic condition or environment is a different molecule. Whether this hemoglobin from hypoxic condition has a higher affinity to oxygen is not yet known. 
Co-Authors . RUSDI Dwirini Retno Gunarti HANIFAH RAHMI KURNIA NUZTIR MANTOLINI RINI PUSPITANINGRUM