Interaction of pepsin with aromatic amino acids and their derivatives immobilized to Sepharose

Abstract

The interaction of porcine pepsin A with immobilized derivatives of aromatic amino acids was investigated. Divinyl sulfone-activated Sepharose was used to immobilize N-acetyl-L-phenylalanine and 3,5-diiodo-L-tyrosine via their free carboxyl groups.

Keywords

• porcine pepsin A
• affinity chromatography
• immobilized derivatives of aromatic amino acids
• thiophilic adsorption chromatography
• gastric-cancer
• affinity-chromatography
• selective adsorption
• binding proteins
• porcine pepsin
• seminal plasma
• human serum
• T-gel
• purification