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Soluble cuticular phenoloxidase in the gypsy moth Lymantria dispar
Author(s) -
Thangaraj Thirumalaisamy,
Aruchami Marappa
Publication year - 1992
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/arch.940210107
Subject(s) - lymantria dispar , enzyme , dispar , tyrosinase , biology , cuticle (hair) , thiourea , gypsy moth , enzyme assay , biochemistry , dithiocarbamate , esterase , larva , botany , microbiology and biotechnology , chemistry , organic chemistry , anatomy , entamoeba histolytica
The soluble enzyme phenoloxidase (tyrosinase) from the larval cuticle of Lymantria dispar has been partially purified using Ultrogel ACA 34, and the activity has been determined using phenolic substrates. The enzyme exhibited more activity toward O‐diphenolic substrates and monophenolic substrates. The enzyme is inhibited by diethyl dithiocarbamate, phenylthiourea, and thiourea. The enzyme has been localized in the 7% slab and disc PAGE as an intense band. The enzyme is suggested to be involved in wound healing. © 1992 Wiley‐Liss, Inc.