Literature DB >> 22096989

[Proteolysis of semax analogues with different N-terminal amino acids by aminopeptidases].

K V Shevchenko, T V V'iunova, I Iu Nagaev, L A Andreeva, L Iu Alfeeva, N F Miasoedov.   

Abstract

Proteolysis of semax (Met-Glu-His-Phe-Pro-Gly-Pro, Sem) and its analogues ([Ala1]Sem, [Gly1]Sem, [Thr1]Sem, [Trp1]Sem) that are differ from semax in substitution of N-terminal Met residue were studied. It is shown that such replacement changes the rate of peptides degradation by N-aminopeptidases (EC 3.4.11.2, Sigma, Type VI, 9.2 units. Akt. / mg). [Ala1]Sem, [Gly1]Sem and [Thr1]Sem semax analogues proved to be more stable to proteolysis than semax (Sem), and their initial product of proteolysis is His-Phe-Pro-Gly-Pro (Sem-5). For triptophan analogue both Glu-His-Phe-Pro-Gly-Pro (Sem-6) and Sem-5 product are formed in similar quantities. It is found that all investigated analogues can be used as inhibitors in Sem proteolysis.

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Year:  2011        PMID: 22096989     DOI: 10.1134/s1068162011040133

Source DB:  PubMed          Journal:  Bioorg Khim        ISSN: 0132-3423


  1 in total

1.  Study of proteolysis of Semax analogues with different N-terminal amino acids by carboxypeptidases.

Authors:  K V Shevchenko; I Yu Nagaev; L A Andreeva; L Yu Alfeeva; N F Myasoedov
Journal:  Dokl Biol Sci       Date:  2013-07-03
  1 in total

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