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  • Title: Differential metabolism of dynorphins in substantia nigra, striatum, and hippocampus.
    Author: Sandin J, Tan-No K, Kasakov L, Nylander I, Winter A, Silberring J, Terenius L.
    Journal: Peptides; 1997; 18(7):949-56. PubMed ID: 9357051.
    Abstract:
    To map the proteolytic enzymes metabolizing dynorphins in brain structures, size-exclusion chromatography linked to electrospray ionization mass spectrometry was used. Enzymes extracted from rat hippocampus, striatum, and substantia nigra were tested for their capability of converting dynorphin-related peptides. Dynorphin A was the most resistant to proteolytic conversion, whereas Big dynorphin and dynorphin B-29 were slowly converted to dynorphin A and dynorphins A and B, respectively. Dynorphin B and alpha-neoendorphin were the least resistant. Dynorphin B was rapidly converted to Leu-enkephalin in the striatum and hippocampus but to Leu-enkephalin-Arg6 in the substantia nigra. alpha-Neoendorphin was converted to Leu-enkephalin in all tissues investigated.
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