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  • Title: Endopeptidase in human cerebrospinal fluid which cleaves proenkephalin B opioid peptides at consecutive basic amino acids.
    Author: Nyberg F, Nordström K, Terenius L.
    Journal: Biochem Biophys Res Commun; 1985 Sep 30; 131(3):1069-74. PubMed ID: 2864927.
    Abstract:
    An endopeptidase releasing the common N-terminal hexapeptide, (Leu)-enkephalin-Arg6, from dynorphins A and B, and alpha-neoendorphin was purified from human cerebrospinal fluid. Purification involved ion-exchange chromatography (DEAE-Sepharose CL-6B), hydrophobic interaction chromatography (phenyl-Sepharose CL-4B) and molecular sieving (Sephadex G-100). The enzyme showed molecular heterogeneity. A major fraction had an apparent molecular weight of about 40,000. It had an optimum activity in the pH range of 6-8. The conversion of dynorphin A was not affected by EDTA or iodoacetate but strongly reduced in the presence of phenylmethyl-sulphonyl fluoride, suggesting the enzyme is a serine protease.
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