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Hematology
Human anion exchanger conformation change is defined
December 29th, 2005
A study from the United States has reported on the conformation change of the cytoplasmic domain of human anion exchanger 1 (cdAE1). "The cdAE1 serves as a center of organization for the red blood cell cytoskeleton as well as several metabolic enzymes and hemoglobin. The protein is known to undergo a reversible pH-dependent conformational change characterized by a 2-fold change in the intrinsic fluorescence and an I I angstrom change in the Stokes radius." "While the exact changes in the molecular structure are unknown, on the basis of the crystal structure of the protein at pH 4.8 and site-directed mutagenesis studies, Zhou and Low have proposed...
Source: Blood Weekly (2005-12-29)
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