A putative processing enzyme from aplysia that cleaves dynorphin A at the single arginine residue Academic Article Article uri icon

Overview

MeSH Major

  • Graft Rejection
  • Kidney Transplantation
  • Primary Graft Dysfunction
  • RNA, Messenger

abstract

  • A peptidase activity cleaving at single arginine residues has been detected in extracts of the atrial gland of Aplysia Californica. The enzyme assay consisted of incubation of enzyme with the mammalian opioid peptide dynorphin A and detection by specific radioimmunoassay of dynorphin (1-8), a single arginine cleavage product. The peptidase activity was characterized following chromatography on DEAE-cellulose. Activity was abolished by a thiol-directed inhibitor and chelators and activated by dithiothreitol and cobalt chloride. The pH optimum was 6.2 in phosphate buffer. Analysis of the products of two substrates suggested that cleavage was occurring on the amino side of the arginine residue.

publication date

  • February 29, 1984

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1016/0006-291X(84)91668-1

PubMed ID

  • 6142711

Additional Document Info

start page

  • 415

end page

  • 22

volume

  • 119

number

  • 1