14517-44-3Relevant articles and documents
Studies of the aminopeptidase proteolysis of semax analogues with different N-terminal amino acid residues
Shevchenko,V'yunova,Nagaev,Andreeva,Alfeeva,Myasoedov
, p. 421 - 427 (2011)
Proteolysis of semax (Met-Glu-His-Phe-Pro-Gly-Pro, Sem) and its analogues with the substitution of Ala, Gly, Thr, or Trp for the N-terminal Met was studied. This substitution was shown to change the degradation rate of these peptides by leucine aminopeptidase (EC 3.4.11.2, Sigma, Type VI, 9.2 activity units/mg). [Ala1]Sem, [Gly1]Sem, and [Thr1]Sem (the semax analogues) proved to be more stable to the proteolysis than semax itself. It was demonstrated that the primary product of the proteolysis was His-Phe-Pro-Gly-Pro (Sem-5). In the case of [Trp1]Sem, the comparable amount of Glu-His-Phe-Pro-Gly-Pro (Sem-6) was found to be formed along with Sem-5. In was established that all the studied semax analogues could be used as inhibitors of its proteolysis. Pleiades Publishing, Ltd., 2011.
Activation of recombinant proteins
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, (2008/06/13)
A process for the activation of recombinant proteins which are present in at least a partially inactive form in which a protein is activated by known solubilization or/and renaturation techniques, said protein having additional helper sequences 2 to 50 amino acids in length at its N- or/and C-terminus whereby the relative hydrophobicity of these helper sequences which is calculated as the sum of the relative hydrophobicity specified in Table 1 for the individual amino acids has a negative numerical value.