Purification, characterization and substrate specificity of a trypsin from the Amazonian fish tambaqui (Colossoma macropomum)

An enzyme was purified from the pyloric caecum of tambaqui (Colossoma macropomum) through heat treatment, ammonium sulfate fractionation, Sephadex® G-75 and p-aminobenzamidine–agarose affinity chromatography. The enzyme had a molecular mass of 23.9kDa, NH2-terminal amino acid sequence of IVGGYECKAHS...

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Veröffentlicht in:	Biochemical and biophysical research communications 2010-06, Vol.396 (3), p.667-673
Hauptverfasser:	Marcuschi, Marina, Espósito, Talita S., Machado, Maurício F.M., Hirata, Izaura Y., Machado, Marcelo F.M., Silva, Márcia V., Carvalho, Luiz B., Oliveira, Vitor, Bezerra, Ranilson S.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Colossoma macropomum Fishes - metabolism FRET peptide Hydrolysis Molecular Sequence Data Processing waste Protease Inhibitors - pharmacology Specific cleavage site Substrate Specificity Tosyl Compounds - pharmacology Tosyllysine Chloromethyl Ketone - pharmacology Tropical fish Trypsin Trypsin - chemistry Trypsin - isolation & purification Trypsin Inhibitors - pharmacology
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