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

Authors :
M. M. B. Van Paassen
I. B. Ginjaar
Glenn E. Morris
G.J.B. van Ommen
J.M. Ellis
Antoon F.M. Moorman
Nguyen thi Man
Alison J. Cartwright
Other departments
Source :
FEBS letters, 272(1-2), 109-112. Wiley-Blackwell
Publisher :
Published by Elsevier B.V.

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.

Details

Language :
English
ISSN :
00145793
Issue :
1-2
Database :
OpenAIRE
Journal :
FEBS Letters
Accession number :
edsair.doi.dedup.....c45af027feb6551995aec2ee914f1660
Full Text :
https://doi.org/10.1016/0014-5793(90)80460-Z