Protyrosinase, from the diapause egg of the grasshopper, Melanoplus differentialis, is activated and converted into tyrosinase by a variety of reagents (Bodine and Carlson, 1940). The active enzyme thus produced has recently been shown to possess similar catalytic properties but to differ greatly in its response to high temperatures (Bodine, Tahmisian, Hill, 1944). The effect of high temperatures is probably related to the type of activator employed as well as to the manner in which the protein enzyme complex is broken down or transformed. Inasmuch as HgCl2, acts as an activator of protyrosinase it becomes of some interest to determine the relative susceptibility to this compound, of the tyrosinase produced by different reagents and to compare this chemical susceptibility with that to high temperatures (Bodine, Tahmisian, Hill, 1944). The present communication deals primarily with the susceptibility of HgCl2, of tyrosinase produced by anionic detergents [sodium dodecyl sulfate, di-ocy1 sodium sulfosuccinate (aerosol OT)], urea and heat (70°C).
Proceedings of the Iowa Academy of Science
©1945 Iowa Academy of Science, Inc.
Bodine, Joseph Hall
"Action of Mercuric Chloride Upon Tyrosinase Produced by Various Activators,"
Proceedings of the Iowa Academy of Science, 52(1), 283-286.
Available at: https://scholarworks.uni.edu/pias/vol52/iss1/40