Analysis of dystrophin in muscular diseases by two-dimensional gel electrophoresis using agarose gels in the first dimension

K. Hamano*, T. Takeya, N. Iwasaki, N. Okoshi, T. Fukubayashi, M. Kirinoki, Y. Yao, T. Hirabayashi, H. Takita

*この研究の対応する著者

研究成果: Article査読

3 被引用数 (Scopus)

抄録

We analyzed dystrophin in cases of normal control, Duchenne muscular dystrophy (DMD), Becker muscular dystrophy (BMD) and infectious muscular disease using two-dimensional gel electrophoresis and immunoblotting with 3 monoclonal dystrophin antibodies : Dys L a mid-rod-domain antibody ; Dys 2, a C-terminal-domain antibody ; and Dys 3, an N-terminal-domain antibody. In cases of normal control, a clearly separated doublet of bands was observed for Dys 1 and 3 at molecular weights 400 and 420 kDa. The isoelectric point was between pH ∼ 5.7-∼ 5.9, similar to that for the myosin heavy chain. In one DMD case, a single faint band was observed for Dys 2. BMD presented a single-band pattern for each antibody. Infectious diseases cases showed 3- to 5-band patterns for Dys 1 and single or no bands for Dys 2 and 3. The pI of the Dys 1 band was almost identical. These results suggest coexistence of normal dystrophin and its proteolytic products, both containing triple helical segment, and show that two-dimensional gel electrophoresis may be applicable in the analysis of dystrophin in muscular disease.

本文言語English
ページ(範囲)102-107
ページ数6
ジャーナルActa Neurologica Belgica
96
2
出版ステータスPublished - 1996
外部発表はい

ASJC Scopus subject areas

  • 臨床神経学

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