Abstract
Alpha(1)-proteinase inhibitor (a,-PI) has been prepared as a concentrate in quantities large enough for clinical testing of its safety and efficacy in the treatment of emphysema and other disorders. The α(1)-PI was purified from Cohn fraction IV-1 paste by polyethylene glycol precipitation and DEAE-Sepharose chromatography. The methods used in the purification are gentle and the resulting product behaves almost identically to the α(1)-PI from plasma. The protein has been heat treated (60°C, 10 h) to lower the risk of transmission of plasma-borne diseases. This resulted in some aggregation of the protein, but did not cause the generation of new antigenic sites. Half-life studies in animals showed that the protein behaved normally (catabolic t(1,2) of 68 h).
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