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Enzyme-catalyzed synthesis of a bioactive oligopeptide in nearly anhydrous solvents with polyethylene glycol-modified proteases

1989; Taylor & Francis; Volume: 1; Issue: 3 Linguagem: Inglês

10.1163/156856290x00044

1568-5624

Akio Nakajima, Yoshiaki Hirano, Tadamasa Terai, Kunio Gotō, Toshio Hayashi, Yoshito Ikada,

Monoclonal and Polyclonal Antibodies Research

An oligopeptide, L-arginyl-glycyl-L-aspartyl-L-serine, having cell attachment activity was synthesized from the respective aminoacids carrying suitable protecting residues, by using carboxymethyl polyethylene glycol (PEG)-modified proteases in organic solvents. Papain, trypsin, and α-chymotrypsin were modified with PEG. Organic solvents used were 1,1,1-trichloroethane, chloroform and chloroform/ ethyl cellosolve (1 : 1) mixture. Identification of the products was done by gel permeation chromatography (GPC) and thin layer chromatography (TLC).