N-terminal degradation of ACTH(4-10) and its synthetic analog semax by the rat blood enzymes.
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.
Potaman
V N
VN
Institute of Molecular Genetics, USSR Academy of Sciences, Moscow.
Alfeeva
L Y
LY
Kamensky
A A
AA
Levitzkaya
N G
NG
Nezavibatko
V N
VN
D000324:Adrenocorticotropic Hormone / Q000031:analogs & derivatives* / Q000097:blood*; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006868:Hydrolysis; D007930:Leucine / Q000031:analogs & derivatives / Q000378:metabolism; D008297:Male; D010446:Peptide Fragments / Q000097:blood*; D051381:Rats; D011919:Rats, Inbred Strains
D010446:Peptide Fragments; C048487:ACTH (4-7), Pro-Gly-Pro-; D000324:Adrenocorticotropic Hormone; D007930:Leucine; C012211:ubenimex; C011394:ACTH (4-10)