Preparation of liposome-coupled NADH and evaluation of its affinity toward formate dehydrogenase based on deactivation kinetics of the enzyme

Colloids and Surfaces B: Biointerfaces

Volumn 109, Issue , 2013, Pages 40-44

  Yoshimoto, Makoto ^a   Kunihiro, Nobutaka ^a   Tsubomura, Naoki ^a   Nakayama, Masaharu ^a  

^a YAMAGUCHI UNIVERSITY   (Japan)

Author keywords

Cofactor bound liposomes; Dialdehyde; Formate dehydrogenase; Membrane interface; Thermostable complex

Indexed keywords

CANDIDA BOIDINII; DEACTIVATION CONSTANTS; DEACTIVATION KINETICS; DIALDEHYDE; FORMATE DEHYDROGENASE; MEMBRANE INTERFACE; NICOTINAMIDE ADENINE DINUCLEOTIDES; THERMOSTABLE COMPLEX;

ENZYMES; LIPOSOMES; MOLECULES; POLYETHYLENE GLYCOLS;

ALDEHYDES;

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; CHEMICAL COMPOUND; FORMATE DEHYDROGENASE; GLUTARALDEHYDE; LIPOSOME; POLY(ETHYLENE GLYCOL)DIALDEHYDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CANDIDA BOIDINII; CHEMICAL BOND; CONTROLLED STUDY; ENZYME INACTIVATION; ENZYME KINETICS; IMMOBILIZATION; MOLECULAR SIZE; NONHUMAN; PRIORITY JOURNAL; SURFACE PROPERTY; THERMOSTABILITY; ZETA POTENTIAL;

CANDIDA; FORMATE DEHYDROGENASES; KINETICS; LIPOSOMES; NAD;

CANDIDA BOIDINII;

EID: 84876735744     PISSN: 09277765     EISSN: 18734367     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2013.03.023     Document Type: Article

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