Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/196502
Type: Artigo de periódico
Title: Metal-binding Proteins Scanning And Determination By Combining Gel Electrophoresis, Synchrotron Radiation X-ray Fluorescence And Atomic Spectrometry.
Author: Verbi, F M
Arruda, S C C
Rodriguez, A P M
Pérez, C A
Arruda, M A Z
Abstract: In the present work, protein bands from in vitro embriogenic callus (Citrus sinensis L. Osbeck) were investigated using micro-synchrotron radiation X-ray fluorescence (muSR-XRF) after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) separation. Metal-binding protein quantification was done after microwave oven decomposition of gel by synchrotron radiation total reflection X-ray fluorescence (SR-TXRF), flame atomic absorption spectrometry (FAAS) and flame atomic emission spectrometry (FAES). According to the analysis of the protein bands, it is possible to observe that both 81 and ca. 14 kDa proteins present different Fe signal intensity at different positions. The analysis of 53 kDa protein, showed even more interesting results. Besides Fe, the muSR-XRF experiments indicate the presence of Ca, Cu, K and Zn. Chemical elements such as Cu, K, Fe and Zn were determined by SR-TXRF, Mg by FAAS and Na by FAES. Ca was determined by SR-TXRF and FAAS only for accuracy check. In the mineralised protein bands of 81 and around 14 kDa band, only Fe was determined (105 and 21.8 microg g(-1)). For those protein bands (86-ca. 14 kDa) were determined, Ca, K, Cu and Zn in a wide concentration range (42.4-283, 2.47-96.8, 0.91-15.9 and 3.39-29.7 microg g(-1), respectively).
Subject: Biophysics
Calcium
Citrus
Copper
Electrophoresis, Polyacrylamide Gel
Metals
Molecular Weight
Potassium
Protein Binding
Proteins
Sodium
Spectrometry, Fluorescence
Spectrophotometry, Atomic
Synchrotrons
Temperature
X-rays
Zinc
Rights: fechado
Identifier DOI: 10.1016/j.jbbm.2004.09.008
Address: http://www.ncbi.nlm.nih.gov/pubmed/15680280
Date Issue: 2005
Appears in Collections:Unicamp - Artigos e Outros Documentos

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