Anil Kumar, P and Sridhar, N (1993) Characterization of phenoloxidase of Penaeus indicus. Indian Journal of Fisheries, 40 (4). pp. 251-255.
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Abstract
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.
Item Type: | Article |
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Uncontrolled Keywords: | Phenoloxidase; Penaeus indicus |
Subjects: | Fish Biotechnology Crustacean Fisheries > Prawn and Prawn fisheries |
Divisions: | CMFRI-Kochi > Physiology and Nutrition Pathology Subject Area > CMFRI > CMFRI-Kochi > Physiology and Nutrition Pathology CMFRI-Kochi > Physiology and Nutrition Pathology Subject Area > CMFRI-Kochi > Physiology and Nutrition Pathology |
Depositing User: | Users 5 not found. |
Date Deposited: | 11 May 2010 08:50 |
Last Modified: | 09 Sep 2015 15:07 |
URI: | http://eprints.cmfri.org.in/id/eprint/498 |
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