Abstract
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 has been prepared. The poly(ethylene glycol) chain confers to the conjugate new physico-chemical properties, including a looser binding to ion exchange chromatographic supports such as CM-Sephadex C-50. The conjugate is thus readily separated from the irreversibly oxidized (unconjugated) forms of the enzyme. A papain preparation titrating 0.97 mol of thiol per mol of enzyme is obtained from the conjugate.
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