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Preparation and Properties of Alpha 1 ‐Proteinase Inhibitor Concentrate from Human Plasma
Author(s) -
Coan M.H.,
Brockway W.J.,
Eguizabal H.,
Krieg T.,
Fournel M.
Publication year - 1985
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1985.tb00193.x
Subject(s) - proteinase inhibitor , alpha (finance) , chromatography , chemistry , polyethylene glycol , sepharose , precipitation , microbiology and biotechnology , biochemistry , enzyme , biology , medicine , surgery , construct validity , physics , meteorology , patient satisfaction
. Alpha 1 ‐proteinase inhibitor (α 1 ‐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‐—I 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).