K. V. Shevchenko1, T. V. V’yunova, I. Yu. Nagaev, L. A. Andreeva, and N. F. Myasoedov
Institute of Molecular Genetics of the Russian Academy of Sciences, 123182 Moscow. Kurchatov pl. 2
Received October 17, 2012; in final form, December 13, 2012
Abstract—Proteolysis of Pro-Gly-Pro-Leu, Pro-Gly-Pro-Gly and Pro-Gly-Pro compared to Met-Glu-His-Phe-
Pro-Gly-Pro (Semax) has been studied. It is shown that all three peptides are significantly more resistant to N-
leucine aminopeptidase (EC 3.4.11.1, Sigma, type VI, 9.2 units/mg), as well as to enzymes of the nasal mucus,
the microsomal fraction of brain, and blood of rats. Metabolites of the proteolysis showed that semax derives
is His-Phe-Pro-Gly-Pro only; Pro-Gly-Pro-Leu forms Gly-Pro-Leu, Pro-Gly-Pro, and Gly-Pro; Pro-Gly-Pro-
Gly gives Pro-Gly-Pro and Gly-Pro; and Pro-Gly-Pro forms Gly-Pro.
Keywords: Semax, glyprolines, membranes of rat brain, degradation of peptides
DOI: 10.1134/S1068162013030151
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