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Monoclonal antibody evidence for structural similarities between the central rod regions of actinin and dystrophin
Author(s) -
Man Nguyen thi,
Ellis J.M.,
Ginjaar I.B.,
van Paassen M.M.B.,
van Ommen G.-J.B.,
Moorman A.F.M.,
Cartwright A.J.,
Morris G.E.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80460-z
Subject(s) - dystrophin , polyclonal antibodies , actinin , antiserum , monoclonal antibody , gene isoform , chemistry , microbiology and biotechnology , western blot , blot , biochemistry , biology , antibody , genetics , cytoskeleton , cell , gene
A monoclonal antibody, MANDYS141, binds to both dystrophin and actinin on Western blots (SDS‐denatured), but only to actinin in frozen sections of human muscle (native conformation). It differs from a polyclonal cross‐reacting antiserum in that it binds to several muscle isoforms of actinin (smooth, fast and slow) from man, mouse and chicken and recognises a quite different part of the proposed triple‐helical region of dystrophin (amino acids 1750–2248). The results suggest that structural homologies between actinin and dystrophin occur more than once in their central helical regions and provide experimental support for an actinin‐like central rod model for dystrophin.