Prophenoloxidase activation in the hemolymph of American cockroach, Periplanata americana
Thangaraj, T.; Subramanium, S.; Vinayakam, A.; Aruchami, M.
Archives Internationales de Physiologie de Biochimie et de Biophysique 100(1): 79-82
ISSN/ISBN: 0778-3124 PMID: 1380338 Accession: 007696801
Prophenoloxidase has been successfully extracted in a stable condition from the hemocytes of Periplanata americana using cane sugar saline solution. Other media used to extract prophenoloxidase were found not suitable. Among the activators used (trypsin, chymotrypsin, sodium oleate and SDS), trypsin activated the proenzyme maximum. Activation during electrophoresis resulted in the dissociation of proenzyme in to two sub-units. The enzyme has also been localised by the agarose gel electrophoresis. The proenzyme was stable up to 50.degree. C and precipitated at 60.degree. C and above. The activated enzyme showed maximum activity at pH 7.0. Preliminary attempt has also been made to precipitate the enzyme protein against the antibody raised in rabbit.