Abstract
Soluble extracts were prepared from adult male and female Haemonchus contortus by differential centrifugation. This extract was fractionated DEAE-cellulose, CM-cellulose, and by sucrose-density-gradient centrifugation. A 20-fold purification from the crude soluble extract was achieved resulting in a preparation having an activity of 5.46 units/mg protein. The enzyme had a pH optimum of 8.0 in Tris-HCl buffer and 6.5 in phosphate buffer and a calculated Michaelis constant of 5.6 × 10 −4 M. The enzyme resembles rabbit muscle and Ascaris suum body wall fructose diphosphate aldolases in the characteristics mentioned above. Metallic ion activators were unnecessary and ethylenediaminetetraacetate did not inhibit activity. Adenosine 5′ triphosphate did inhibit the Haemonchus aldolase as had been reported for rabbit muscle aldolase. The latter substance was reported to activate Ascaris muscle aldolase.
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