Isoforms of a dynorphin B converting enzyme isolated by column electrophoresis in agarose suspension.
A dynorphin B converting enzyme previously purified from bovine spinal cord was subjected to column electrophoresis in agarose suspension. By this technique combined with HPLC gel filtration it was possible to resolve and recover several isoforms of the proteinase. All these isoenzymes were associated with a similar molecular size but apparently they differed with regard to their net charges. No significant difference between their inhibitory profiles or their Km values for the release of Leu-enkephalin-Arg6 from dynorphin B was observed.
Silberring
J
J
Department of Pharmacology, University of Uppsala, Sweden.
Nyberg
F
F
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D004399:Dynorphins / Q000031:analogs & derivatives*; D004587:Electrophoresis, Agar Gel; D004723:Endorphins; D004743:Enkephalin, Leucine / Q000031:analogs & derivatives / Q000378:metabolism; D006902:Hydroxymercuribenzoates / Q000494:pharmacology; D007526:Isoelectric Point; D007527:Isoenzymes / Q000302:isolation & purification; D007700:Kinetics; D008970:Molecular Weight; D013116:Spinal Cord / Q000201:enzymology
D004723:Endorphins; D006902:Hydroxymercuribenzoates; D007527:Isoenzymes; C030601:4-hydroxymercuribenzoate; D004743:Enkephalin, Leucine; D004399:Dynorphins; C026768:enkephalin-Leu, Arg(6)-; C036200:rimorphin; D003546:Cysteine Endopeptidases; C063078:dynorphin converting enzyme