Conformational differences between native and recombinant horseradish peroxidase revealed by tritium planigraphy

Biochemistry (Moscow)

Volumn 68, Issue 11, 2003, Pages 1225-1230

  Orlova, M A ^a   Chubar, T A ^a   Fechina, V A ^a   Ignatenko, O V ^a   Badun, G A ^a   Ksenofontov, A L ^a   Uporov, I V ^a   Gazaryan, I G ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Labeled compounds; Native horseradish peroxidase; Recombinant horseradish peroxidase; Tritium; Tritium activation; irradiation

Indexed keywords

AMINO ACIDS; CATALYSIS; CHEMICAL ACTIVATION; CONFORMATIONS; DOSIMETRY; HYDROPHILICITY; HYDROPHOBICITY; NUMERICAL ANALYSIS; PROTEINS; RADIOACTIVITY; SWELLING; TRITIUM;

CATALYTIC HISTIDINE; NATIVE HORSERADISH PEROXIDASE; OLIGOSACCHARIDES; RECOMBITANT HORSERADISH PEROXIDASE; THERMAL ACTIVATION; TRITIUM PLANIGRAPHY;

ENZYMES;

ARMORACIA RUSTICANA;

AMINO ACID; HORSERADISH PEROXIDASE; RECOMBINANT PROTEIN; TRITIUM;

ARTICLE; CHEMISTRY; ENZYME STABILITY; GAMMA RADIATION; GENETICS; ISOLATION AND PURIFICATION; PROTEIN CONFORMATION; RADIATION EXPOSURE;

AMINO ACIDS; ENZYME STABILITY; GAMMA RAYS; HORSERADISH PEROXIDASE; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; TRITIUM;

EID: 0742286267     PISSN: 00062979     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:BIRY.0000009137.75375.d2     Document Type: Article

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