Purification, characterization and biosynthesis of parabutoxin 3, a component of Parabuthus transvaalicus venom

European Journal of Biochemistry

Volumn 269, Issue 7, 2002, Pages 1854-1865

  Huys, Isabelle ^a   Dyason, Karin ^b   Waelkens, Etienne ^a   Verdonck, Fons ^a   Van Zyl, Johann ^c   Plessis, Johan Du ^b   MüLler, Gert J ^c   Van Der Walt, Jurg ^b   Clynen, Elke ^a   Schoofs, Liliane ^a   Tytgat, Jan ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

^b NORTH WEST UNIVERSITY   (South Africa)

^c STELLENBOSCH UNIVERSITY   (South Africa)

Author keywords

Parabuthus; Purification; Scorpion; Synthesis; Toxin

Indexed keywords

AMINO ACID; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; PARABUTOXIN 3; POTASSIUM CHANNEL; POTASSIUM CHANNEL BLOCKING AGENT; SCORPION VENOM; SYNTHETIC DNA; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BACTERIAL CELL; CELL MEMBRANE POTENTIAL; CONCENTRATION RESPONSE; CONTROLLED STUDY; CYTOPLASM; DISULFIDE BOND; DRUG MECHANISM; ELECTROPHYSIOLOGY; ESCHERICHIA COLI; GEL FILTRATION; GENETIC CODE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; SCORPION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DNA PRIMERS; ION CHANNEL GATING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POTASSIUM CHANNEL BLOCKERS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SCORPION VENOMS; SCORPIONS; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

ANIMALIA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PARABUTHUS; PARABUTHUS TRANSVAALICUS; SCORPIONES; STAPHYLOCOCCUS PHAGE 3A; SYNTHETIC CONSTRUCT; XENOPUS LAEVIS;

EID: 85047696278     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.02833.x     Document Type: Article

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