Identification and partial characterisation of a serum enzyme which hydrolyses epidermal inhibitory pentapeptide.
We have identified an enzyme present in mammalian, avian, and reptilian serum which cleaves epidermal inhibitory pentapeptide (pGlu-Glu-Asp-Ser-GlyOH) to form a relatively stable tripeptide (pGlu-Glu-Asp). The enzyme has an inhibitor profile unlike any readily identifiable serum enzyme, and is stable at 4 degrees C for up to 3 months. As most experiments using the pentapeptide are carried out in the presence of serum this finding may have important implications on future research into the biological function of the pentapeptide.
Whitehead
P A
PA
Department of Dental Surgery, University of Leeds, England.
Robinson
P A
PA
Hume
W J
WJ
Keen
J N
JN
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001717:Birds; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000097:blood*; D006131:Growth Inhibitors / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D008322:Mammals; D009842:Oligopeptides / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D011761:Pyrrolidonecarboxylic Acid / Q000031:analogs & derivatives; D014426:Turtles
D000596:Amino Acids; D006131:Growth Inhibitors; D009842:Oligopeptides; D011480:Protease Inhibitors; C050550:epidermal pentapeptide; D010450:Endopeptidases; D011761:Pyrrolidonecarboxylic Acid