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|Type:||Artigo de periódico|
|Title:||Ion mobility mass spectrometry: an elegant alternative focusing on speciation studies|
|Abstract:||This work is proposed to demonstrate the Traveling-Wave Ion Mobility Specrometry (TWIMS) coupled to Mass Spectrometry (MS) as an alternative technique for speciation analysis between metals/metalloids and biomolecules. Mobilities of bovine carbonic anhydrase bound to Ba(2+), Cu(2+), Pb(2+), Zn(2+), Cr(3+), Cr(6+), Se(4+) and Se(6+) were estimated. The metal belonging to the bovine carbonic anhydrase structure, commonly found in the commercially available enzyme, was removed by filtration, using centrifugal filter devices. Then, some metals/metalloids were added to 10.0 mmol L(-1) ammonium acetate at pH = 6.8 enzyme solution. Experiments were carried out by direct insertion of the sample at 10 mu L min(-1) flow rate into the ESI source of the instrument. Carbonic anhydrase mobility varied according to the metal bound in its structure, following the order: Zn(2+) < Cu(2+) < Ba(2+) < Pb(2+). Metals with higher affinity by the enzyme, such as Zn(2+) and Cu(2+) had lower mobility, suggesting a higher structural modification, binding itself to the enzyme metallic site. Considering metals with different oxidation states, the enzyme mobility followed the order: Se(4+) < Cr(6+) < Se(6+) < Cr(3+).|
|Editor:||Royal Soc Chemistry|
|Citation:||Journal Of Analytical Atomic Spectrometry. Royal Soc Chemistry, v. 26, n. 1, n. 201, n. 206, 2011.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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