Two distinct variants of erythrocyte spectrin beta IV domain.
We report two distinct variants affecting the beta IV domain of erythrocyte spectrin, designated spectrin Saint-Chamond and spectrin Tlemcen. They were discovered in a French family and an Algerian individual, respectively. They appeared clinically and morphologically asymptomatic in the heterozygous state. In two-dimensional maps of spectrin partial digests, both mutants were manifested by cathodic shifts (with no change of the molecular weights) of the peptides that cover the N-terminal region of spectrin beta IV domain. The relevance of the abnormal peptides to the beta IV domain was established by quantitative analysis and by Western blotting using anti-beta IV domain-specific antibodies. These two variants are thus far the most distal variants of spectrin to be defined on an unequivocal structural basis.
Pothier
B
B
Génétique Moléculaire de la Membrane Erythrocytaire, Faculté de Médecine Grange-Blanche, Lyon, France.
Alloisio
N
N
Morlé
L
L
Maréchal
J
J
Barthélemy
H
H
Ducluzeau
M T
MT
Dorier
A
A
Delaunay
J
J
D000328:Adult; D015153:Blotting, Western; D004912:Erythrocytes / Q000166:cytology; D014644:Genetic Variation; D006801:Humans; D008297:Male; D009154:Mutation; D010449:Peptide Mapping; D013049:Spectrin / Q000235:genetics* / Q000276:immunology
D013049:Spectrin