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Biophysical characterization of alanine aminotransferase from Trypanosoma cruzi
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نویسنده
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de moraisa s.b. ,de arruda campos brasil de souza t. ,weiler a.v.p. ,murakami m.t.
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منبع
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protein and peptide letters - 2016 - دوره : 23 - شماره : 12 - صفحه:1118 -1122
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چکیده
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Aminotransferases are an important group of enzymes that catalyze the transfer of an amino group of an amino acid into a keto acid. alanine aminotransferase from trypanosoma cruzi (tcalat) was cloned,overexpressed and purified. far-uv circular dichroism (cd),dynamic light scattering (dls),analytical size exclusion chromatography (asec) and small angle x-ray scattering (saxs) provide data concerning tcalat biophysical behavior. cd analysis displayed a typical spectrum of α-β proteins analogously as observed for other alanine aminotransferases. the protein is stable until 40°c and above that temperature starts to denatured. its temperature of melting is equal to 50°c. dls,asec and saxs data show that protein is monomeric in solution. all these gather initial information on secondary and quaternary structures of tcalat. © 2016 bentham science publishers.
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کلیدواژه
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Alanine aminotransferases; Biophysical characterization; Enzyme; Quaternary structure; Secondary structure; Trypanosoma cruzi
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آدرس
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carlos chagas institute,fiocruz-pr,rua algacyr munhoz mader,3775,curitiba, Brazil, carlos chagas institute,fiocruz-pr,rua algacyr munhoz mader,3775,curitiba, Brazil, carlos chagas institute,fiocruz-pr,rua algacyr munhoz mader,3775,curitiba, Brazil, brazilian biosciences national laboratory,brazilian center for research in energy and materials,campinas, Brazil
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Authors
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s.b. ,t. ,a.v.p. ,m.t.
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