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. 1970 Aug;118(5):713-8.
doi: 10.1042/bj1180713.

Purification and amino acid sequence of melanocyte-stimulating hormone from the dogfish Squalus acanthias

P J Lowry, A Chadwick

Purification and amino acid sequence of melanocyte-stimulating hormone from the dogfish Squalus acanthias

P J Lowry et al. Biochem J. 1970 Aug.

Abstract

A melanocyte-stimulating hormone (MSH) was isolated by gel filtration and ion-exchange chromatography from extracts of the pituitary glands of dogfish. Sequence studies were carried out on the hormone and its enzymically and chemically cleaved fragments. The sequence of the hormone, Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Met, shows that ten of its 11 residues are the same as ten of the 13 residues of mammalian alpha-MSH. About half of its molecules have the carboxyl group at the C-terminus free and about half are amidated; about a fifth have an extra tyrosine residue on the N-terminus, thereby making 11 residues the same as in mammalian alpha-MSH. Unlike the mammalian hormone, however, none of it was found to be N-acetylated.

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