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Molecular characterization of commercial porcine factor VIII concentrate
P Lollar, CG Parker and RP Tracy
Department of Medicine, University of Vermont College of Medicine,
Burlington.
Commercial porcine factor VIII concentrate (Hyate:C) is effective in
treatment of patients with hemophilia A who have circulating antibodies to
factor VIII. The molecular forms of factor VIII in the concentrate were
identified and evaluated in light of the known properties of porcine and
human factor VIII. The factor VIII in the concentrate was isolated by
tandem chromatography on gelatin-Sepharose and monoclonal anti-factor
VIII-Sepharose. The factor VIII was 1% of the protein mass of the
concentrate when calculated by either quantity of protein recovered or by
radioimmunoassay. Both functional assay and Western blotting of the crude
concentrate indicated that maximum coagulant function was achieved by
proteolytic activation of procofactor forms of factor VIII. The factor VIII
can be fractionated by cation-exchange high-performance liquid
chromatography (HPLC) into two or three species of heterodimers depending
on the lot. The specific activity of the purified porcine factor VIII was
550 U/mg using pooled porcine plasma at 1 U/mL as a standard. From this
value, a factor VIII concentration in normal pig plasma of 2 micrograms/mL
was calculated. This agreed well with a value of 3 micrograms/mL obtained
by radioimmunoassay (RIA) of factor VIII in porcine plasma. In contrast,
reported values for human factor VIII average 5800 U/mg, resulting in a
calculated concentration in plasma of 0.2 microgram/mL. The finding that
porcine plasma contains a significantly higher circulating mass of factor
VIII than human plasma appears to explain previous difficulties in
comparing porcine and human factor VIII in standard assays.
Volume 71,
Issue 1,
pp. 137-143,
01/01/1988
Copyright © 1988 by The American Society of Hematology
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