Abstract:
Three drtferent serine protease Inhibitors were Isolated from camel plasma and purified to apparent
homogeneity. The purification was achieved using (NH.hSO. predplation, affinity chromatography on Blue Sephal"O$e,Ionexchange
chromatography on DEAE-Sephadex A-50 at pH 8.0 and 6.5, gel filtration on Sephacryl S200 and
polyacrylamide gel electrophoresis (PAGE). Inhibitor I and II were found to Inhibit trypsin and chymotrypsln whiM! Inhlblor III
Inhibited trypsin only, with no detectable chymotrypsin Inhibition. Inhibitor I was found to be analogous to human a,-
protease inhibitor with relative molecular mass of 58,000, it inhibited trypsin and chymotrypsin at a 1:1 molar ratio. The
Inhibitor was resistant to heat for 30 minutes at S·C and retillned only 16.7% of Its activity at 70·C for 1OrTin~es, The
Inhibitor had a maximum Inhibitory activity at pH 8.0, however, no detectable Inhlbitlon was observed at pH 5.0 and 6.0.
This study Indicated that Inhibitor I exhibited similar properties to human ai-protease inhlbitor
