title: Purification of the pro-phenol oxidase enzyme from haemocytes of the cockroach Blaberus discoidalis.
abstract: 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.
authors.affiliation: School of Biological Sciences, University College of Swansea, Singleton Park, Wales, U.K.
authors.forename: H J
authors.initials: HJ
authors.lastname: Durrant
authors.forename: N A
authors.initials: NA
authors.lastname: Ratcliffe
authors.forename: C R
authors.initials: CR
authors.lastname: Hipkin
authors.forename: A
authors.initials: A
authors.lastname: Aspan
authors.forename: K
authors.initials: K
authors.lastname: Söderhäll
mesh_terms: 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*
chemical_list: D004792:Enzyme Precursors; D014442:Monophenol Monooxygenase