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dc.contributor.authorKrittikorn Kümpornsinen_US
dc.contributor.authorSurasak Jiemsupen_US
dc.contributor.authorSuganya Yongkiettrakulen_US
dc.contributor.authorThanat Chookajornen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherThailand National Center for Genetic Engineering and Biotechnologyen_US
dc.identifier.citationBiochemical and Biophysical Research Communications. Vol.406, No.3 (2011), 332-335en_US
dc.description.abstractThe elastic property of red blood cell is supported by interaction between red cell membrane and the intricate cytoskeleton network underlying the membrane bilayer cytoplasmic face. One of the major scaffold protein linkers is band 3-ankyrin complex. Defects occurring in this complex have been found in many inherited diseases, causing red blood cell abnormalities. Here we combined the power of mass spectrometry with conventional biochemical purification methods in order to study the native interactions among band 3, ankyrin and Protein 4.2. This approach provided in vivo evidence for the association between band 3 and N-terminal ankyrin purified directly from the cell membrane. The C-terminal regions of ankyrin were not found to be a stable partner of the band 3 complex. Protein 4.2 was shown here to be an integral part of the complex. Its association to the band 3-ankyrin complex could withstand harsh purification conditions. Our findings lend additional support to the interaction between band 3 and ankyrin N-terminal domain previously shown by in vitro binding assays and provide evidence for a band 3 core complex comprising of band 3, ankyrin and Protein 4.2. © 2011 Elsevier Inc.en_US
dc.rightsMahidol Universityen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleCharacterization of band 3-ankyrin-Protein 4.2 complex by biochemical and mass spectrometry approachesen_US
Appears in Collections:Scopus 2011-2015

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