No abstract

An extracorporeal reactor containing a packed bed of Dacron fibers has been developed. Escherichia coli II L-asparaginase was coupled to the Dacron using gamma-aminopropyltriethoxysilane and glutaraldehyde. The preparation had an activity of 37 IU per gram of Dacron (37 degrees C). The apparent Km was studied as a function of the flow rate. The data indicated that the apparent Km approached the Km of the native enzyme at flow rates of about 300 mg/min. In vivo use of L-asparaginase immobilized on the Dacron indicated effective lowering of plasmatic L-asparagine levels.