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This study investigated the effects of peptide apelin-12 (H-Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Met-Pro-Phe-OH, A12) and its novel structural analog (H-(NαMe)Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Nle-Pro-Phe-OH, AI) on myocardial antioxidant enzyme activities, lipid peroxidation, and reactive oxygen species formation in ex vivo and in vivo models of(More)
Apelin-12 and a number of its analogues (Nle10-, MeArg1, Nle10, MeArg1, Nle10, Phe12-NH2-, Arg1(NO2), Nle10, Phe12-NH2-), resistant to the degradation of proteases, were synthesized by the Fmocmethod of SPPS. By-products of synthesis were examined. It was found that the serine hydroxyl group was sulfating during the final deprotection of apelin-12 and its(More)
65 INTRODUCTION The adipocytokine apelin peptide, which consists of 77 amino acid residues, and its APJJreceptor conn nected with GGproteins of membranes of endothelial cells and cardiomyocytes participate in regulation of the tone of coronary blood vessels and contractility of the myocardium [1]. CCterminal fragments of the pepp tide (apelinn12, 13, and(More)
The effects of C-terminal fragment of natural peptide apelin-12 H-Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Met-Pro-Phe-OH (A12) and its structural analog H-(NαMe)Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Nle-Pro-Phe-OH (AI) on Cu2+-induced free radical oxidation of low-density lipoprotein in human blood plasma and activity of commercially available enzymes superoxide(More)
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