Structure of barley grain peroxidase refined at 1.9-A resolution. A plant peroxidase reversibly inactivated at neutral pH. | J Biol Chem;273(4): 2241-8, 1998 Jan 23. | MEDLINE

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Structure of barley grain peroxidase refined at 1.9-A resolution. A plant peroxidase reversibly inactivated at neutral pH.

Henriksen, A; Welinder, K G; Gajhede, M.

Affiliation

Henriksen A; Department of Physical Chemistry, University of Copenhagen, København O, Denmark. anette@jerne.ki.ku.dk

J Biol Chem ; 273(4): 2241-8, 1998 Jan 23.

Article in En | MEDLINE | ID: mdl-9442067

Subject(s)

Peroxidases/chemistry; Crystallography, X-Ray; Hydrogen-Ion Concentration; Models, Molecular; Protein Conformation; Protein Structure, Secondary

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Collection: 01-internacional Database: MEDLINE Main subject: Peroxidases Type of study: Prognostic_studies Language: En Journal: J Biol Chem Year: 1998 Document type: Article Affiliation country: Denmark

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Collection: 01-internacional Database: MEDLINE Main subject: Peroxidases Type of study: Prognostic_studies Language: En Journal: J Biol Chem Year: 1998 Document type: Article Affiliation country: Denmark