Glucagon in Perfused Rat Pancreas

نویسندگان

  • KEVIN J. O'CONNOR
  • ADRIAN GAY
  • NORMAN R. LAZARUS
چکیده

The biosynthesis of glucagon was studied by using the recirculated, isolated perfused rat pancreas. [3H]Tryptophan was initially incorporated into acid-ethanol-extractable protein, which on gel filtration was eluted with a molecular weight ofabout 9000 and contained a small amount of glucagon immunoreactivity. With longer incubation [3H]tryptophan incorporation into a second peak was obtained in an identical position with that of the majority of rat glucagon immunoreactivity. This peak of labelled protein exhibited migration characteristics on polyacrylamide-gel electrophoresis identical with those of rat glucagon and was identified as newly synthesized glucagon by demonstration ofspecific binding and dissociation behaviour with glucagon antibodies. The incorporation of [3H]tryptophan into acid-ethanol-extractable protein was inhibited by cycloheximide. High concentrations of glucose increased [3H]tryptophan incorporation into highmolecular-weight protein but decreased incorporation into proteins smaller than cytochrome c. The pattern of [3H]leucine incorporation into protein was similar to that of [3H]tryptophan.

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تاریخ انتشار 2005