Abstract
A procedure for the purification of guanine deaminase inhibitor from human brain mitochondria is described. The inhibitor was enriched about 150-fold with recoveries of over 65%. It is nondialyzable, insoluble in water, and stable for over 30 days at -16 degrees C. However, the protein is completely inactivated at 50 degrees C in 5 min. The purified protein also inhibits the activities of a number of other enzymes.
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