Abstract
An aspartic proteinase was isolated from the culture filtrate of Claviceps purpurea by a method which includes affinity chromatography on immobilized inhibitor pepstatin, gel filtration and ion-exchange chromatography. The isolated enzyme was electrophoretically homogenous, had a molecular weight between 41,000 and 43,000 and pI 4.60. It was most active toward hemoglobin at pH 3.5. The enzyme was unstable above pH 7. It was completely inhibited by pepstatin, whereas diazoacetyl norleucine methyl ester and epoxy(p-nitrophenoxy)propan inactivated the enzyme by 40%.
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