Characterization of substance P(1-7) and (1-8) generating enzyme in human cerebrospinal fluid.

A substance P-hydrolyzing endopeptidase has been purified from a large quantity of human cerebrospinal fluid by ion exchange chromatography (DEAE-Sepharose CL-6B) and molecular sieving (Sephadex G-100 and Sephacryl S-200). The purification was monitored by measuring the conversion of synthetic substance P using a radioimmunoassay specific for its (1-7) fragment. The enzyme has an apparent molecular weight of 43,000. It cleaves predominantly at the Phe7-Phe8 and Phe8-Gly9 bonds but gives no or negligible conversion of the other tachykinins, neuromedin K and L (substance K).