Enzymological studies of melanotropins

Ana Maria de L. Castrucci, Mac E. Hadley, Tomi K. Sawyer, Victor J. Hruby

Research output: Contribution to journalArticlepeer-review

52 Scopus citations

Abstract

1. 1. The relative stability of natural melanotropins and related synthetic analogues to serum and purified proteolytic enzymes was studied. 2. 2. Both α- and β-MSH were rapidly inactivated by frog serum, but much more slowly by rat serum. β-MSH was more stable than α-MSH to serum inactivation. 3. 3. Both α- and β-MSH were rapidly inactivated by α-chymotrypsin and trypsin. 4. 4. The synthetic analogues, [Nle4, d-Phe7]-α-MSH and and [Cys4,Cys10]-α-MSH, were totally resistant to inactivation by frog and rat serum enzymes. 5. 5. [Nle4, d-Phe7]-α-MSH was resistant to inactivation by α-chymotrypsin and trypsin, whereas [Cys4,Cys10]-α-MSH, was partially resistant to these enzymes under similar conditions. 6. 6. Melanotropin analogues resistant to inactivation by serum enzymes may prove useful in a variety of physiological studies wherein natural melanotropins would be rapidly inactivated.

Original languageEnglish (US)
Pages (from-to)519-524
Number of pages6
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume78
Issue number3
DOIs
StatePublished - 1984

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology

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