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Proteolysis of simple glyprolines by leucine aminopeptidase and enzymes from nasal mucus, brain membranes, and blood of rats

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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.

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Abbreviations

MERB:

membrane enzymes of rat brain

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Correspondence to K. V. Shevchenko.

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Original Russian Text © K.V. Shevchenko, T.V. V’yunova, I.Yu. Nagaev, L.A. Andreeva, N.F. Myasoedov, 2013, published in Bioorganicheskaya Khimiya, 2013, Vol. 39, No. 3, pp. 320–325.

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Shevchenko, K.V., V’yunova, T.V., Nagaev, I.Y. et al. Proteolysis of simple glyprolines by leucine aminopeptidase and enzymes from nasal mucus, brain membranes, and blood of rats. Russ J Bioorg Chem 39, 283–287 (2013). https://doi.org/10.1134/S1068162013030151

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  • DOI: https://doi.org/10.1134/S1068162013030151

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