Properties of Folate Binding Protein Purified from Cow’s Milk

Subandrate, Subandrate and Gunarti, Dwirini Retno and Sadikin, Mohamad Properties of Folate Binding Protein Purified from Cow’s Milk. HAYATI Journal of Biosciences. ISSN 2086-4094

[img] PDF (Jurnal dr. Subandrate, M.Biomed) - Submitted Version
Restricted to Repository staff only

Download (136Kb)

    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 DEAEcellulose 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 β-mercaptoethanol treatment. In contrary, the folate binding didn need Ca2+ ion, as indicated by EDTA test which gave the same result as control.

    Item Type: Article
    Subjects: R Medicine > RZ Other systems of medicine
    Divisions: Faculty of Medicine
    Depositing User: dr, Subandrate M.Biomed
    Date Deposited: 25 Jun 2014 10:07
    Last Modified: 25 Jun 2014 10:07
    URI: http://eprints.unsri.ac.id/id/eprint/4515

    Actions (login required)

    View Item