Collagenase covalently attached to cellulose acetate membranes, following periodate activation of the membrane, maintained its enzymatic activity and permanence of attachment for more than 6 weeks. The length of spacer between the enzyme and the membrane was studied with enzymes attached directly, through ethylenediamine and through ethylenediamine plus succinnic anhydride. Enzyme activity was measured by determining the degradation rate of a pigskin gelatin solution, and stability of the bond was measured by observing continued degradation after the enzyme-membrane was removed from the solution. The longest spacer resulted in the highest enzyme activity. I nterest is growing rapidly in supplying blood glucose control in diabetics through the use of chambers in which Islets of Langerhans are interfaced with the blood supply through a permeable membrane. The object is to provide adequate insulin release in response to blood glucose, while isolating the cells from immune response. Consideration is being given to both intravascular and extravascular islet-transplantation chambers. A problem that arises in the consideration of an extravascular device is that synthetic materials placed in the body tissues rapidly become covered with cells (polymorphonuclear leukocytes and macrophages) and surrounded with relatively impervious fibrous tissue. This could decrease the diffusion rates of glucose and insulin, eventually rendering a chamber useless. One possible solution to this problem is the attachment of proteolytic enzymes to the surface of the chamber to prevent formation and attachment of fibrous tissue at the interface. It was reported by Jolley (1 ) that a cellulosic chamber (Millipore Corporation) coated with covalently bound collagenase and implanted in the rat
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