Characterization of extrachromosomal DNA in the flesh fly Sarcophaga bullata

Chromosoma ◽  
1979 ◽  
Vol 75 (2) ◽  
pp. 145-159 ◽  
Author(s):  
David Samols ◽  
Hewson Swift
1987 ◽  
Vol 65 (5) ◽  
pp. 1158-1166 ◽  
Author(s):  
F. Michael Barrett

A tyrosinase, enzyme A, and a laccase, enzyme B, have been partially purified from larval cuticle of the flesh fly Sarcophaga bullata. Enzyme A (EC 1.10.3.1, o-diphenol: O2 oxidoreductase) oxidizes o-diphenols but not p-diphenols, is strongly inhibited by phenylthiourea, and has a pH optimum around pH 6.5–7.0. Assays on intact cuticle suggest that it becomes maximally activated at pH between 8 and 9. Enzyme B (EC 1.10.3.2, p-diphenol: O2 oxidoreductase) oxidizes both o-diphenols and p-diphenols, is not inhibited by phenylthiourea but is inhibited by concentrations of sodium azide that have little effect on enzyme A, and has a pH optimum near pH 4.5. Enzyme A was identified in extracts of cuticle from nine other species representing five orders. Enzyme B was much less readily extractable but was partially purified from larval cuticle of Phormia regina, Musca domestica, and Lucilia sericata. A summary of all species studied to date makes possible the test of a hypothesis about the distribution of these cuticular phenoloxidases within the Insecta.


1975 ◽  
Vol 23 (11) ◽  
pp. 800-807 ◽  
Author(s):  
P L Chang ◽  
P E Morrison

Trehalase activity in flight muscle of the flesh fly Sacrophaga bullata is detected histochemically at light- and electron-microscopic levels by using diaminobenzidine, glucose oxidase and peroxidase in the incubation medium. The association of trehalase activity with the inner mitochondrial membrane is confirmed. Biochemical assay shows that about 50% of the initial total trehalase activity is lost from the tissue during the histochemical processing and about 50% remains for histochemical detection.


Sign in / Sign up

Export Citation Format

Share Document