Studies on Molecular Weights of Two Peptide Hormones from the Urophysis of White Sucker (Catostomus commersoni)

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Abstract
The molecular weights of two active principles extracted from the urophysis of the teleost fish Catostomus commersoni in 0.1 N HCl or in 0.25% acetic acid have been investigated by gel filtration chromatography and SDS–polyacrylamide gel electrophoresis. Two peptides with urotensin I (long-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 without 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.

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