Synthetic Octapeptide Inhibitor of Cathepsin D

Rapid isolation of cathepsin D by affinity chromatography on the immobilized synthetic inhibitor

“…The octapeptide inhibitor was coupled by its amino terminal side, which enables positioning of its active part at a distance from the solid, matrix. Although the inhibition constant of the inhibitor (Ki = 5.2 X lo4 M) was slightly higher than, for example, the Michaelis constant for hemoglobin substrate (KM = 2.7 X lo-' M) [9] the affinity column effectively worked. FEBSLETTERS November 1976 In a separate experiment it was found that the Acknowledgements non-specific hydrophobic adsorption to the sixcarbon spacer is of minor importance.…”

“…We have found that synthetic octapeptide Gly-Glu-Gly-Phe-Leu-Gly-DPhe-I_eu is a competitive inhibitor of cathepsin D [9]. This report describes its use as an affinity ligand for the simple and rapid isolation of cathepsin D from tissue extracts in a single or double step procedure.…”