Abstract

Studies were made on proteolytic activity for homogenates of larval Boophilus microplus ticks. Maximal activity was recorded at pH 3–3.5 in the 27,000g supernatant fraction. Hydrolysis of bovine serum albumin was inhibited by excess substrate; the optimum concentration was 0.8 mg%. Enzymatic activity was linear with time up to 100 min of incubation and with protein concentration up to 12.5 mg/ml. A slight stimulation of activity by the monovalent cations Na + and K + was demonstrated, with maximum stimulation at 60 m M concentration. Maximal specific activity was found in homogenates from 9-day-old larvae. Gel filtration of the 27,000g supernatant fraction by Sephadex G-100 chromatography showed three peaks and a shoulder in 4-day-old larvae and only one peak in 40-day-old larvae. Specific activity was found to be greatest in the 27,000g fraction, while the 105,000g and the soluble fraction had similar activities.

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