Purification of the pro-phenol oxidase enzyme from haemocytes of the cockroach Blaberus discoidalis.
Pro-phenol oxidase was purified from the haemocytes of the cockroach Blaberus discoidalis by Blue Sepharose chromatography, hydrophobic-interaction chromatography on a Phenyl-Superose column and, finally, gel filtration on a Superose 6 column. Results suggest that the molecule exists as a polymer of identical 76 kDa monomeric units. The enzyme is a glycoprotein with pI of 5.2 and can be converted by trypsin into phenol oxidase.
Durrant
H J
HJ
School of Biological Sciences, University College of Swansea, Singleton Park, Wales, U.K.
Ratcliffe
N A
NA
Hipkin
C R
CR
Aspan
A
A
Söderhäll
K
K
D000818:Animals; D002853:Chromatography, Liquid; D003058:Cockroaches; D004591:Electrophoresis, Polyacrylamide Gel; D004792:Enzyme Precursors / Q000097:blood / Q000302:isolation & purification*; D005260:Female; D006434:Hemocytes / Q000201:enzymology*; D007525:Isoelectric Focusing; D008297:Male; D014442:Monophenol Monooxygenase / Q000097:blood / Q000302:isolation & purification*
D004792:Enzyme Precursors; D014442:Monophenol Monooxygenase