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Latent larval cuticular phenoloxidase in the coconut pest, Oryctes rhinoceros
Author(s) -
Longankumar Kandasamy,
Thangaraj Thirumalaisamy,
Manimegalai Muthusamy,
Aruchami Marappa,
Vinayakam Anandhan
Publication year - 1996
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1996)33:1<27::aid-arch2>3.0.co;2-u
Subject(s) - biology , thermolysin , chymotrypsin , trypsin , enzyme , biochemistry , rhinoceros , proteolytic enzymes , tyrosinase , botany , microbiology and biotechnology , zoology
Cuticular phenoloxidase (Tyrosinase) in the larval stage of the coconut pest Oryctes rhinoceros has been extracted in the stable proform using cane sugar saline/borate buffer. The extracted prophenol oxidase can be activated by the addition of proteolytic enzymes such as trypsin, chymotrypsin, thermolysin, and subtilisin. Detergents such as SDS and Tween‐80 also activated the enzyme. Electrophoretical analysis revealed dissociation of the enzyme into two molecular forms after its activation by proteolytic enzymes. The functional significance of the enzyme is suggested to involve the generation of quinone compounds in the wound healing process: most phenoloxidase inhibitors prevented melanization when applied topically to surgical wounds. © 1996 Wiley‐Liss, Inc.