Analysis of the Subsite Specificity of Rat Insulysin Using Fluorogenic Peptide Substrates

Recombinant rat insulysin was shown to cleave the internally quenched fluorogenic peptide 2-aminobenzyl-GGFLRKVGQ-ethylenediamine-2,4-dinitrophenol at the R–K bond, exhibiting a Km of 13 μm and a Vmax of 2.6 μmol min−1mg−1. Derivatives of this peptide in which the P2 leucine or the P2‘ valine were r...

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Veröffentlicht in:	The Journal of biological chemistry 2001-01, Vol.276 (2), p.1152-1155
Hauptverfasser:	Song, Eun-Suk, Mukherjee, Atish, Juliano, Maria Aparecida, Pyrek, Jan St, Goodman, Jack P., Juliano, Luiz, Hersh, Louis B.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Binding Sites Chromatography, High Pressure Liquid Dinitrophenols - pharmacokinetics Hydrolysis Insulysin - metabolism Kinetics Oligopeptides - chemistry Oligopeptides - metabolism Oligopeptides - pharmacokinetics Rats Recombinant Proteins - metabolism Substrate Specificity
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