Small-molecule reductants inhibit multicatalytic activity of AA-NADase from Agkistrodon acutus venom by reducing the disulfide-bonds and Cu(II) of enzyme

Biopolymers

Volumn 93, Issue 2, 2010, Pages 141-149

  Zhang, Li Yun ^a   Xu, Xiao Long ^a   Luo, Zhao Feng ^a   Wu, Hao ^a   Shen, Deng Ke ^a   Peng, Li Li ^a   Liu, Yang Zhong ^a  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

Author keywords

AA NADase; Agkistrodon acutus; ATPase; Cu(II); Disulfide bond; DTT; GSH; L ascorbate; TCEP

Indexed keywords

CYSTEINE RESIDUES; DITHIOTHREITOL; ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY; ENDOGENOUS INHIBITOR; GLUTATHIONES; ISOTHERMAL TITRATION CALORIMETRY; L-ASCORBATE; PEPTIDE CHAIN; POLYACRYLAMIDE GEL ELECTROPHORESIS; REDUCTANTS; SMALL MOLECULES; TRIS(2-CARBOXYETHYL) PHOSPHINE;

CHROMATOGRAPHIC ANALYSIS; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTROPHORESIS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PARAMAGNETIC RESONANCE; PARAMAGNETISM; PHOSPHORUS COMPOUNDS; SPECTROSCOPY; ZINC; ZINC COMPOUNDS;

ENZYMES;

AA NAD GLYCOHYDROLASE; ADENOSINE TRIPHOSPHATASE; APO AA NADASE; APYRASE; ASCORBIC ACID; CUPRIC ION; CUPROUS ION; CYSTEINE; DIMER; DITHIOTHREITOL; GLUTATHIONE; NICOTINAMIDE ADENINE DINUCLEOTIDE NUCLEOSIDASE; NUCLEOSIDASE; PHOSPHINE; REDUCING AGENT; UNCLASSIFIED DRUG; VENOM; ZINC ION; ASCORBATE OXIDASE; TRIS(2 CARBOXYETHYL)PHOSPHINE;

AGKISTRODON; AGKISTRODON ACUTUS; ARTICLE; DISULFIDE BOND; ELECTRON SPIN RESONANCE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ISOTHERMAL TITRATION CALORIMETRY; NONHUMAN; POISONOUS SNAKE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CLEAVAGE; REDUCTION; RESIDUE ANALYSIS; CATALYSIS; CHEMICAL MODIFICATION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME ACTIVE SITE; MOLECULE;

DEINAGKISTRODON ACUTUS;

ANIMALS; COPPER; CROTALID VENOMS; CYSTEINE; DISULFIDES; DITHIOTHREITOL; GLUTATHIONE; NAD+ NUCLEOSIDASE; OXIDATION-REDUCTION; PHOSPHINES;

EID: 73649084011     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.21312     Document Type: Article

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