by venous blood. The remaining 93% of CO 2 diffuse into RBCs where the gas is either bound to hemoglobin in the carbamate form, or is converted by RBC enzyme carbonic anhydrase (CA) into carbonic acid, which in turn dissociates into an H ϩ ion and an HCO 3 Ϫ ion [8, 9]. The conversion of approximately 70% of CO 2 to HCO 3 Ϫ ions in the circulation serves two important physiological functions. Firstly, it provides a more effi cient means of transport of CO 2 from tissue cells to the lungs. Secondly, the HCO 3 Ϫ ions produced act in a buffer system for metabolic acids. In the absence of a catalyst, the conversion of CO 2 to H ϩ and HCO 3 Ϫ is a very slow reaction. Thus, CO 2 and carbonic acid exist in the blood in a ratio of 400:1, and the proportion of CO 2 to HCO 3 Ϫ is 20:1 [10]. The hydration reaction of CO 2 would therefore occur much too slowly to be of physiological importance were it not for the presence of the zinc-containing metalloenzyme carbonic anhydrase (CA) in the RBCs [11, 12]. CA is involved in the crucial process of CO 2 transport by catalyzing the reversible hydration of CO 2 to carbonic acid, H ϩ and HCO 3 Ϫ , thus playing a fundamental role in the maintenance of acid-base balance of the body.While antioxidant enzymes such as superoxide dismutase (SOD) and catalase (CAT) have been crosslinked with PolyHb to produce oxygen carriers that can confer antioxidant properties [13], CA has not been incorporated into a PolyHb-enzyme system in suffi cient amount for the transport of CO 2 . The aim of this study is thus to prepare