C. Paul et al., PREPARATION AND CHARACTERIZATION OF A S-MONOMETHOXYPOLY-(ETHYLENE GLYCOL) THIODERIVATIVE OF PAPAIN, Phytochemistry, 35(6), 1994, pp. 1413-1417
A derivative of papain in which the free thiol group of the proteinase
is attached to a poly(ethylene glycol) chain via a disulphide bond ha
s been prepared. The poly(ethylene glycol) chain confers to the conjug
ate new physicochemical properties, including a looser binding to ion
exchange chromatographic supports such as CM-Sephadex C-50. The conjug
ate is thus readily separated from the irreversibly oxidized (unconjug
ated) forms of the enzyme. A papain preparation titrating 0.97 mol of
thiol per mol of enzyme is obtained from the conjugate.