Purification of recombinant flavanone 3beta-hydroxylase from petunia hybrida and assignment of the primary site of proteolytic degradation.

Lukacin, R; Gröning, I; Schiltz, E; Britsch, L; Matern, U

Lukacin, R; Gröning, I; Schiltz, E; Britsch, L; Matern, U.

Affiliation

Lukacin R; Institut für Pharmazeutische Biologie, Philipps-Universität Marburg, Deutschhausstrasse 17A, Marburg, D-35037, Germany.

Arch Biochem Biophys ; 375(2): 364-70, 2000 Mar 15.

Article in En | MEDLINE | ID: mdl-10700394

Subject(s)

Mixed Function Oxygenases/isolation & purification; Mixed Function Oxygenases/metabolism; Plants/enzymology; Amino Acid Sequence; Blotting, Western; Buffers; Catalysis/drug effects; Chromatography, Gel; Chromatography, Ion Exchange; Endopeptidases/metabolism; Enzyme Stability/drug effects; Escherichia coli/genetics; Mass Spectrometry; Mixed Function Oxygenases/chemistry; Molecular Sequence Data; Molecular Weight; Peptide Fragments/chemistry; Peptide Fragments/isolation & purification; Peptide Fragments/metabolism; Plant Proteins/chemistry; Plant Proteins/isolation & purification; Plant Proteins/metabolism; Protease Inhibitors/pharmacology; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Sequence Analysis, Protein; Time Factors

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Collection: 01-internacional Database: MEDLINE Main subject: Plants / Mixed Function Oxygenases Language: En Journal: Arch Biochem Biophys Year: 2000 Document type: Article Affiliation country: Germany Country of publication: United States

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