Abstract
A search for low molecular weight peptide substrates for the metalloendoproteinase, human fibroblast stromelysin, resulted in the discovery that substance P (Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-LeuMet-NH 2) is a substrate for this enzyme and is cleaved exclusively at the Gln 6-Phe 7 bond. On the basis of this observation, a semicontinuous HPLC-based assay was developed that monitors the production of the hydrolysis product, fragment 7–11 (SP 7–11 ). Steady-state velocities for the production of SP 7–11 have been determined as a function of substrate concentration and obey simple, Michaelis-Menten kinetics. For a 1-ml reaction volume, V max = (2.4 nmol SP 7–11/min)/ μg protein and K m = 0.38 mM.
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