Anil Kumar, P and Sridhar, N (1993) Characterization of phenoloxidase of Penaeus indicus. Indian Journal of Fisheries, 40 (4). pp. 251-255.
The enzyme phenoloxidase from haemolymph of Penaeus indicus was partially purified us- ing ammonium sulphate fractionation technique. An overall recovery of 52% with a 5-fold purification was achieved. Dialysis reduced the enzyme activity indicating the presence of dialysable cofactors. The enzyme had high afinity for the biphenolic substrate adrenalin fol- lowed by dopamine, catechol and dopa. The rate of the reaction was linear up to 3 min when adrenalin was used as the substrate. The enzyme had an optimum tem erature of 50°C but lost 60% of its activity when heated to 70°C for 10 min. The Krn and t"max of the enzyme with adrenalin as the substrate was 0.122 mM and 0.588 OD unitslmg protein a min respectively. The enzyme was inhibited by the substrate adrenalin at a concentration of IS mM and by cupric salts. Magnesium and calcium stimulated the enzyme activity. EDTA and mercaptoethanol strongly inhibited the enzyme.
|Uncontrolled Keywords:||Phenoloxidase; Penaeus indicus|
Crustacean Fisheries > Prawn and Prawn fisheries
|Divisions:||CMFRI-Cochin > Physiology and Nutrition Pathology|
|Deposited By:||INVALID USER|
|Deposited On:||11 May 2010 14:20|
|Last Modified:||11 May 2010 14:20|
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