Tissue distribution and characterization of peptide C-terminal alpha-amidating activity in rat.
The C-terminal alpha-amide formation of peptides is one of the most important events in prohormone processing. Recently, we developed a simple and sensitive assay for detecting alpha-amidating activity in tissues by using (125I)-Ac-Tyr-Phe-Gly as a substrate. Using this assay method, we have determined the tissue distribution of alpha-amidating enzyme activity in adult male rat. High concentrations of alpha-amidating activity were found in pituitary, brain, thyroid, gastrointestinal tract, pancreas, heart, submaxillary glands and parotid glands. Alpha-amidating enzyme activities in all tissues examined exhibit very similar copper and ascorbate requirements, pH dependence, and behavior on gel-filtration.
D000577:Amides / Q000378:metabolism*; D000818:Animals; D001205:Ascorbic Acid / Q000494:pharmacology; D003300:Copper / Q000494:pharmacology; D008297:Male; D010455:Peptides / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D014018:Tissue Distribution
D000577:Amides; D010455:Peptides; D003300:Copper; D001205:Ascorbic Acid