Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Morita, Y.
Right arrow Articles by Minami, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Morita, Y.
Right arrow Articles by Minami, J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1988, Vol. 103, No. 4 693-699
© 1988 Japanese Biochemical Society

research-article

Purification, Crystallization, and Characterization of Peroxidase from Coprinus cinereus

Yuhei Morita*, Honami Yamashita*, Bunzo Mikami*, Hiroyuki Iwamoto*, Shigeo Aibara*, Masaki Terada** and Junichi Minami**

* Research Institute for Food Science, Kyoto University Uji, Kyoto 611
** Central Institute of Nissin Shokuhin Co. Ritto-cho, Shiga 620-30

Peroxidase (donor: H2O2 oxidoreductase [EC 1.11.1.7 [EC] ]) was purified from a culture broth of an inkcap Basidiomycete, Coprinus cinereus S.F. Gray. A single component containing a low amount of carbohydrate was isolated by affinity chromatography on concanavalin A-Sepharose and crystallized from ammonium sulfate solution. The enzyme is an acidic protein (pl 3.5) and consists of a single polypeptide chain having the molecular weight of 41,600 daltons. The enzyme contains one protohemin per molecule and exhibits the characteristic absorption, circular dichroism, and magnetic circular dichroism spectra of a heme-protein. The Coprinus peroxidase forms two characteristic intermediate compounds, I and II, and the rate constants for hydrogen peroxide and guaiacol had similar values to those for higher plant peroxidases. The ferric enzyme formed a cyanide compound with a dissociation constant similar to those for higher plant enzyme, but the dissociation constant of the ferrous enzyme-cyanide was large. The chemical composition of Coprinus peroxidase showed 381 amino acid residues, 1 glucosamine, 3 true sugars, 3 calcium, and 1 non-heme iron other than 1 protohemin. The secondary structure of the fungal enzyme was very similar to that of horseradish peroxidase.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Appl. Environ. Microbiol.Home page
R. Ullrich, J. Nuske, K. Scheibner, J. Spantzel, and M. Hofrichter
Novel Haloperoxidase from the Agaric Basidiomycete Agrocybe aegerita Oxidizes Aryl Alcohols and Aldehydes
Appl. Envir. Microbiol., August 1, 2004; 70(8): 4575 - 4581.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
M. Heinzkill, L. Bech, T. Halkier, P. Schneider, and T. Anke
Characterization of Laccases and Peroxidases from Wood-Rotting Fungi (Family Coprinaceae)
Appl. Envir. Microbiol., May 1, 1998; 64(5): 1601 - 1606.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
K. Fukuyama, K. Sato, H. Itakura, S. Takahashi, and T. Hosoya
Binding of Iodide to Arthromyces ramosus Peroxidase Investigated with X-ray Crystallographic Analysis, 1H and 127I NMR Spectroscopy, and Steady-state Kinetics
J. Biol. Chem., February 28, 1997; 272(9): 5752 - 5756.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Fukuyama, N. Kunishima, F. Amada, T. Kubota, and H. Matsubara
Crystal Structures of Cyanide- and Triiodide-bound Forms of Arthromyces ramosus Peroxidase at Different pH Values
J. Biol. Chem., September 15, 1995; 270(37): 21884 - 21892.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.