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. 1991 Apr 30;176(2):741-6.
doi: 10.1016/s0006-291x(05)80247-5.

N-terminal degradation of ACTH(4-10) and its synthetic analog semax by the rat blood enzymes

V N Potaman  1 , L Y Alfeeva, A A Kamensky, N G Levitzkaya, V N Nezavibatko
Affiliations

N-terminal degradation of ACTH(4-10) and its synthetic analog semax by the rat blood enzymes

V N Potaman et al. Biochem Biophys Res Commun. .

Abstract

Degradation of a regulatory peptide ACTH(4-10) and its synthetic analog semax in rat blood and serum was studied using high-performance liquid chromatography. About one third to one half of the serum degrading activity could be ascribed to bestatin-sensitive aminopeptidase which cleaved first and second N-terminal residues Met and Glu producing relatively stable intermediates. Comparable areas under the degradation/accumulation curves for intact peptides and intermediates implied that the latter can contribute to effects of intact peptides. Semax turned out to be more stable than ACTH(4-10) against the action of other enzymes that took part in degradation.

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