title: Studies on molecular weights of two peptide hormones from the urophysis of white sucker (Catostomus commersoni).
abstract: The molecular weights of two active principles extracted from the urophysis of the teleost fish Catostomus commersoni in 0.1 N HC1 or in 0.25% acetic acid have been investigated by gel filtration chromatography and SDS-polyacrylamide gel electrophoresis. Two peptides with urotensin I Tlong-acting rat hypotensive) activity and two peptides with urotensin II (fish smooth muscle stimulating) activity were found by these procedures. The smaller of the two urotensin I peptides (molecular weight 1200-1700), designated urotensin Is, was shown to be a fragment of the larger peptide (molecular weight 2300-3000) which is produced by acid hydrolysis withour loss of rat hypotensive activity. The two urotensin II peptides are suggested to represent either a monomer and a dimer or open and closed forms of a peptide.
mesh_terms: D000818:Animals; D001681:Biological Assay; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005399:Fishes; D006728:Hormones / Q000302:isolation & purification / Q000494:pharmacology; D008970:Molecular Weight; D009132:Muscles / Q000187:drug effects / Q000502:physiology; D009490:Neurosecretory Systems / Q000032:analysis*; D010455:Peptides / Q000302:isolation & purification / Q000494:pharmacology; D051381:Rats
chemical_list: D006728:Hormones; D010455:Peptides