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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/11578
Title: Characterization of band 3-ankyrin-Protein 4.2 complex by biochemical and mass spectrometry approaches
Authors: Krittikorn Kümpornsin
Surasak Jiemsup
Suganya Yongkiettrakul
Thanat Chookajorn
Mahidol University
Thailand National Center for Genetic Engineering and Biotechnology
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 18-Mar-2011
Citation: Biochemical and Biophysical Research Communications. Vol.406, No.3 (2011), 332-335
Abstract: The 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.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=79952739522&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/11578
ISSN: 10902104
0006291X
Appears in Collections:Scopus 2011-2015

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