Characterization of a Bromoperoxidase From the Marine Algae Penicillus Capitatus
type: CreativeWork
description: The soluble emzyme bromperoxidase isolated from the marine green algae P. capitatus is capable of catalyzing halide oxiations while in the presence of peroxide. Protein purification and characterization of this enzyme showed that the prosthetic group is ferric protoporphyrin IX and that the enzyme consists of two equal molecular weight subunits whose combined weight is approximately 100,000. Bromoperoxidase contains no detectable level of carbohydrate.
abstract: The soluble emzyme bromperoxidase isolated from the marine green algae P. capitatus is capable of catalyzing halide oxiations while in the presence of peroxide. Protein purification and characterization of this enzyme showed that the prosthetic group is ferric protoporphyrin IX and that the enzyme consists of two equal molecular weight subunits whose combined weight is approximately 100,000. Bromoperoxidase contains no detectable level of carbohydrate.
author: Manthey, John Anthony
keywords: Biophysics, General
date published: 2014-12-15T23:43:49Z
date modified: 2026-07-22T22:26:03Z
provider: University of Illinois - Urbana-Champaign
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Illinois at Urbana-Champaign

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2142/70537