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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Alloisio, N. Articles by Kastally, R. Search for Related Content PubMed PubMed Citation Articles by Alloisio, N. Articles by Kastally, R. Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Spectrin Jendouba: an alpha II/31 spectrin variant that is associated with elliptocytosis and carries a mutation distant from the dimer self- association site N Alloisio, R Wilmotte, L Morle, F Baklouti, J Marechal, MT Ducluzeau, L Denoroy, C Feo, BG Forget and R Kastally CNRS URA 1171, Faculte de Medecine Grange-Blanche, Lyon, France. Spectrin Jendouba (alpha II/31) was found in a Tunisian family. In the heterozygous state, it is associated with asymptomatic elliptocytosis and a minimal defect in spectrin dimer self-association. On partial digestion of spectrin with trypsin, an abnormal cleavage appeared following Lys 788. Peptide and DNA sequencing indicated that the responsible mutation is alpha 791 Asp----Glu (GAC----GAA). As in most alpha-spectrin variants associated with elliptocytosis, the change alters helix 3 of the proposed triple helical model of spectrin structure. Modified helix 3 in repeat alpha 8 is the most distant from the N-terminus of alpha-spectrin in known variants associated with elliptocytosis. Volume 80, Issue 3, pp. 809-815, 08/01/1992 Copyright © 1992 by The American Society of Hematology CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

	Copyright © 1992 by American Society of Hematology         Online ISSN: 1528-0020