%0 Journal Article
%T Properties of Folate Binding Protein Purified from Cow¡¯s Milk
%A SUBANDRATE
%A DWIRINI RETNO GUNARTI
%A MOHAMAD SADIKIN
%J HAYATI Journal of Biosciences
%D 2012
%I The Indonesian Biological Society & Bogor Agricultural University
%X 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¨CSH or imidazol group in its active site. The importance of disulfide bridge was proven by decreasing of folate binding capacity of FBP after  -mercaptoethanol treatment. In contrary, the folate binding didn need Ca2+ ion, as indicated by EDTA test which gave the same result as control.
%K folate binding protein
%K folic acid
%K binding capacity
%U http://journal.ipb.ac.id/index.php/hayati/article/view/5621/4265