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. 1990 Oct 15;272(1-2):109-12.
doi: 10.1016/0014-5793(90)80460-z.

Monoclonal antibody evidence for structural similarities between the central rod regions of actinin and dystrophin

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Monoclonal antibody evidence for structural similarities between the central rod regions of actinin and dystrophin

T M Nguyen et al. FEBS Lett. .
Free article

Abstract

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.

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