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

T. M. Nguyen; J. M. Ellis; I. B. Ginjaar; M. M. van Paassen; G. J. van Ommen; A. F. Moorman; A. J. Cartwright; G. E. Morris

doi:https://doi.org/10.1016/0014-5793(90)80460-Z

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

T. M. Nguyen, J. M. Ellis, I. B. Ginjaar, M. M. van Paassen, G. J. van Ommen, A. F. Moorman, A. J. Cartwright, G. E. Morris

Other Departments

Research output: Contribution to journal › Article › Academic › peer-review

21 Citations (Scopus)

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

Original language	English
Pages (from-to)	109-112
Journal	FEBS letters
Volume	272
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(90)80460-Z
Publication status	Published - 1990

Access to Document

https://doi.org/10.1016/0014-5793(90)80460-Z

Cite this

@article{bf31b7ad30e0484aade56869eed37468,

title = "Monoclonal antibody evidence for structural similarities between the central rod regions of actinin and dystrophin",

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",

author = "Nguyen, {T. M.} and Ellis, {J. M.} and Ginjaar, {I. B.} and {van Paassen}, {M. M.} and {van Ommen}, {G. J.} and Moorman, {A. F.} and Cartwright, {A. J.} and Morris, {G. E.}",

year = "1990",

doi = "https://doi.org/10.1016/0014-5793(90)80460-Z",

language = "English",

volume = "272",

pages = "109--112",

journal = "FEBS letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "1-2",

}

TY - JOUR

T1 - Monoclonal antibody evidence for structural similarities between the central rod regions of actinin and dystrophin

AU - Nguyen, T. M.

AU - Ellis, J. M.

AU - Ginjaar, I. B.

AU - van Paassen, M. M.

AU - van Ommen, G. J.

AU - Moorman, A. F.

AU - Cartwright, A. J.

AU - Morris, G. E.

PY - 1990

Y1 - 1990

N2 - 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

AB - 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

U2 - https://doi.org/10.1016/0014-5793(90)80460-Z

DO - https://doi.org/10.1016/0014-5793(90)80460-Z

M3 - Article

C2 - 1699800

SN - 0014-5793

VL - 272

SP - 109

EP - 112

JO - FEBS letters

JF - FEBS letters

IS - 1-2

ER -