Arginine-to-lysine substitutions influence recombinant horseradish peroxidase stability and immobilisation effectiveness

BMC Biotechnology

Volumn 7, Issue , 2007, Pages

  Ryan, Barry J ^a   Ó'Fágáin, Ciarán ^a  

^a DUBLIN CITY UNIVERSITY   (Ireland)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE RESIDUE; ARGININE-TO-LYSINE SUBSTITUTIONS; HORSERADISH PEROXIDASE; MUTANT;

AMINO ACIDS; BIOINFORMATICS; BIOTECHNOLOGY; CATALYST ACTIVITY; PLANTS (BOTANY); POLYPEPTIDES;

ENZYME IMMOBILIZATION;

ARGININE; HORSERADISH PEROXIDASE; LYSINE; POLYETHERSULFONE; RECOMBINANT HORSERADISH PEROXIDASE; SEPHAROSE; UNCLASSIFIED DRUG; IMMOBILIZED ENZYME; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BIOINFORMATICS; BIOTECHNOLOGICAL PROCEDURES; BIOTECHNOLOGICAL PRODUCTION; CATALYSIS; ENZYME IMMOBILIZATION; ENZYME STABILITY; MUTANT; PROTEIN STRUCTURE; WILD TYPE; BINDING SITE; BIOSYNTHESIS; CHEMISTRY; GENETICS; SITE DIRECTED MUTAGENESIS; ULTRASTRUCTURE;

ARMORACIA RUSTICANA;

AMINO ACID SUBSTITUTION; ARGININE; BINDING SITES; CATALYSIS; ENZYME STABILITY; ENZYMES, IMMOBILIZED; HORSERADISH PEROXIDASE; LYSINE; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS;

EID: 38949107919     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-7-86     Document Type: Article

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