Isolation and Partial Characterization of Buffalo Plasma Fibronectin (Fn)

Jagati, R., Paliwal, S., Siddiqui, M.Z., Kumar, S., Sharma, A. K. and Kumar, A. 1995. Isolation and partial characterization of buffalo plasma fibronectin (Fn). J. Appl. Anim. Res., 8: 97-104. Fibronectin (Fn) a large extracellular adhesive glycoprotein was isolated from buffalo plasma using gelatin-sepharose affinity chromatography and characterized by analytical SDS-PAGE, GPC-HPLC and amino acid analysis. Analytical GPC-HPLC revealed homogeneity of the isolate with a molecular weight of 460 kD and SDS-PAGE analysis of Fn in reduced form depicted presence of two 230 kD polypeptide chains linked by disulphide bonds. Microchemical analysis of the Fn hydrolysate using 6N HCl gave the amino acid composition similar to that of other species except a higher content of arginine (R) i.e. 8.2% as compared to 5.3% in other species. Staphylococcus aureus cells showed preferential binding to Fn coated surface.