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Association studies of erythoid α‐spectrin at the tetramerization site
Author(s) -
Lam Vinh Q.,
Antoniou Chloe,
Rolius Ramunas,
Fung Leslie W.M.
Publication year - 2009
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.2009.07876.x
Subject(s) - spectrin , tetramer , mutant , mutation , epb41 , genetics , genetic association , association (psychology) , chemistry , biology , medicine , biochemistry , gene , genotype , psychology , single nucleotide polymorphism , cell , cytoskeleton , psychotherapist , enzyme
Summary The functional roles of residues 21–43 and 55–59 in the α‐spectrin N‐terminal region in forming tetramers were determined by the introduction of mutations at each of these positions. We measured association affinities for tetramer formation (K d ), which can be used to predict clinical severity, of these mutants. A total of nine residues critical for association with β‐spectrin were found. The mutations of six of these residues have already been known to cause hereditary elliptocytosis or hereditary pyropoikilocytosis. Clinical symptoms associated with three mutations of residues 23, 57 and 58 have not yet been reported. We suggest that these mutations may also introduce abnormalities to erythrocytes.