Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Maya Boyanova"'
Publikováno v:
Biotechnology & Biotechnological Equipment. 26:170-174
Glycation of recombinant human interferon-gamma (rhIFN-γ) causes conformational alterations of the molecule and results in reduction of its biologic activity. The aim of this study was to find adeq...
Publikováno v:
Biotechnology & Biotechnological Equipment. 24:1904-1909
Glycation is a non-emzymatic reaction between free amino groups and reducing sugars (16), which was shown to take place also in human (13). It causes severe complications in diabetic and uremic patients, whereas in normal subjects contributes to sene
Publikováno v:
Biotechnology & Biotechnological Equipment. 23:1063-1067
Recombinant human interferon-gamma (rhIFN-γ) produced in Escherichia coli (E. coli) undergoes structural and functional alterations as a result of two different but parallel processes—aggregation and non-enzymatic glycosylation (glycation). Findin
Publikováno v:
Biotechnology & Biotechnological Equipment. 21:177-181
The effect of temperature, mechanical stress and surface tension on fluorescence and biological activity of recombinant human interferon gamma (rhIFN-γ) was studied. All three physical factors caused a similar decrease of fluorescence intensity and
Publikováno v:
Biotechnology & Biotechnological Equipment. 21:215-219
Equations were derived describing the fluorescence intensity of IFNy solutions on the basis of a dimer-monomers equilibrium of the native protein. The experimental data were found to fit very well the theoretical values predicted by these equations.
Publikováno v:
Analytical Biochemistry. 308:178-181
Autor:
Stefan Petrov, Ivan Ivanov, Maya Boyanova, Genoveva Nacheva, Alfredo Berzal-Herranz, Andrey Karshikoff
Publikováno v:
Scopus-Elsevier
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC. Repositorio Institucional del CSIC
instname
Interferon-gamma (IFNγ) accomplishes its multiple biological effects by activating the STAT transcription factors, which are translocated to the nucleus through a specific nuclear localization sequence(s) (NLS) located in the IFNγ molecule. Two put
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ff1e370bb36428bcfc74c2fa057f41e
http://hdl.handle.net/10261/143763
http://hdl.handle.net/10261/143763
Publikováno v:
National Institute of Allergy and Infectious Diseases, NIH ISBN: 9781934115770
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d9b4b4354fb1e9d4a9e4e041a9aa41d
https://doi.org/10.1007/978-1-59745-569-5_41
https://doi.org/10.1007/978-1-59745-569-5_41
Publikováno v:
The Journal of biological chemistry. 278(51)
Until recently, nonenzymatic glycosylation (glycation) was thought to affect the proteins of long living eukaryotes only. However, in a recent study (Mironova, R., Niwa, T., Hayashi, H., Dimitrova, R., and Ivanov, I. (2001) Mol. Microbiol. 39, 1061-1
Autor:
Ivan Ivanov, Kristina Todorova, Maya Boyanova, Genoveva Nacheva, Andrey Karshikoff, Alfredo Berzal-Herranz
Publikováno v:
Archives of biochemistry and biophysics. 413(1)
The significance of the C-terminal part of human interferon gamma (hIFNgamma) for its biological activity was studied by 3(')-end gene mutagenesis. A series of nine derivative genes obtained by systemic deletion of three codons was constructed and ex