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The World of Protozoa, Rotifera, Nematoda and Oligochaeta

Ref ID : 7661

C. Auriault and M. Desmazeaud; [Inventaire des Differentes Activites Proteolytiques chez Acanthamoeba culbertsoni et Acanthamoeba rhysodes Cultivees sur Milieu Axenique: Mise en Evidence D'activites Amino Peptidasiques Intra et Extra Cellulaires]. Protistologica XV(1):123-128, 1979

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An endocellular acidic proteasic activity has been shown in A. culbertsoni and A. rhysodes and is able to hydrolyse hemoglobin. The existence of distinct endocellular and exocellular amino-peptidase activities according to their pH optimum activity has also been revealed for these same stocks. These amino peptidases are able to hydrolyse the dipeptide synthetics substrates that have been utilized. Addition in the culture of mouse nervous or pulmonary material does not lead to new exocellular proteases and peptidases synthetis induction. These different proteases and peptidases may be involved in the phenomenon of pathogenesis. The exocellular amino-peptidases in A. culbertsoni may participate in the swift destruction mechanism of host cells. Proteases and peptidases could likewise be utilized as a simple and rapid means of determining different amoeba stocks of the genus Acanthamoeba.