Abstract
The reactivity and the role of sulphydryl groups in adenosine deaminase have been investigated. In the sodium dodecylsulphate-denatured enzyme 2.1 sulphydryl groups are titratable with p-mercuribenzoate. The native enzyme is inactivated by p-mercuribenzoate or phenylmercuric acetate and a stoichiometric relationship exists between the equivalents of mercaptide formed and the inactivation of the enzyme. Substrate analogs protect the enzyme againstp-mercuribenzoate and phenylmercuric acetate inactivation. Iodoacetamide, iodoacetate, and N-ethylmaleimide, which do not affect the enzyme activity, do not react with sulphydryl groups. The results show that a sulphydryl group unreactive towards the alkylating reagents is essential in some way for the enzymatic activity. The lack of reactivity of the essential sulphydryl group with alkylating reagents suggests that the sulphydryl group may be contained in a hydrophobic region of the enzyme molecule.
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