کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1987541 1540289 2010 12 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Role of tyrosine 33 residue for the stabilization of the tetrameric structure of human cytidine deaminase
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Role of tyrosine 33 residue for the stabilization of the tetrameric structure of human cytidine deaminase
چکیده انگلیسی
In the present work the effect of a mutation on tyrosine 33 residue (Y33G) of human cytidine deaminase (CDA) was investigated with regard to protein solubility and specific activity. Osmolytes and CDA ligands were used to increase the yield and the specific activity of the protein. The mutant enzyme was purified and subjected to a kinetic characterization and to stability studies. These investigations reinforced the hypothesis that in human CDA the side chain of Y33 is involved in intersubunit interactions with four glutamate residues (E108) forming a double latch that connects each of the two pairs of monomers of the tetrameric CDA.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 47, Issue 4, 1 November 2010, Pages 471-482
نویسندگان
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