Epidermal inhibitory pentapeptide phosphorylated in vitro by calf thymus protein kinase NII is protected from serum enzyme hydrolysis.
In this paper, we demonstrate that synthetic epidermal mitosis inhibiting pentapeptide (pyroGlu-Glu-Asp-Ser-Gly) is phosphorylated in vitro at serine level by protein kinase NII isolated from calf thymus chromatin. A serum enzyme, which rapidly cleaves the synthetic epidermal mitosis inhibiting pentapeptide, also hydrolyses the synthetic transcription inhibiting pentapeptide (pyroGlu-Ala-Glu-Ser-Asn). The phosphorylated forms of both pentapeptides are protected from the serum enzyme activity.
Bramucci
M
M
Department of Molecular, Cellular and Animal Biology, University of Camerino, Italy.
Miano
A
A
Amici
D
D
D000595:Amino Acid Sequence; D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D002417:Cattle; D006131:Growth Inhibitors / Q000378:metabolism; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011761:Pyrrolidonecarboxylic Acid / Q000031:analogs & derivatives; D012694:Serine / Q000378:metabolism; D013950:Thymus Gland / Q000378:metabolism*
D001798:Blood Proteins; D006131:Growth Inhibitors; D009842:Oligopeptides; C073613:pyroglutamyl-alanyl-glutamyl-seryl-asparagine; C050550:epidermal pentapeptide; D012694:Serine; D011494:Protein Kinases; C026813:protein kinase NII; D011761:Pyrrolidonecarboxylic Acid