Bovine Serum Albumin Inter-chain Disulphide Bridges Determination Using Urea-PAGE

  • Hezekiah Fatoki Fatoki Department of Biochemistry, Federal University of Technology, P.M.B. 704, Akure, Nigeria

Abstract

Bovine Serum Albumin (BSA) is a protein composed of 583 amino acid residues. It has three similar domains which are predominantly a-helical (70%) and include loops and a large number of disulphide bridges. Disulphide bridges stabilize chain folding and multichain structure. This study aimed at investigating the number of inter-chain disulphide bridges present in BSA. Urea Polyacrylamide Gel Electrophoresis (Urea-PAGE) approach was used to count the number of disulphide bridges present in BSA. Two bands were obtained which showed that the denatured, reduced and alkylated BSA has two chains which are linked together by a disulfide bridge. Keywords: Bovine serum Albumin (BSA), Urea-PAGE, Disulphide bridges, Alkylation,

Author Biography

Hezekiah Fatoki Fatoki, Department of Biochemistry, Federal University of Technology, P.M.B. 704, Akure, Nigeria
Department of Biochemistry, Federal University of Technology, P.M.B. 704, Akure, Nigeria

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Published
2017-03-29
Section
Article