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. 1997 Jul 14;138(1):81–93. doi: 10.1083/jcb.138.1.81

Figure 6.

Figure 6

Dystrophin and utrophin complexes contain distinct pairs of syntrophin isoforms. (A) Dystrophin and utrophin complexes were immunoaffinity purified from Triton-solubilized extracts of mouse skeletal muscle with antibodies DYS3669 and UTR3165, respectively. Sample loadings were adjusted to contain approximately equal amounts of syntrophin, as judged by immunoblotting (pan-Syn, mAb SYN1351). Duplicate blots were probed with mAbs Mandys-8 (Dys), and DRP-1 (Utr) or biotinylated polyclonal antibodies SYN17 (α1-syn), SYN37 (β1-syn), and SYN28 (β2-syn). (B) Syntrophins were immunoaffinity purified from skeletal muscle extracts with Abs SYN17, SYN37, and SYN28. Sample loadings were adjusted to contain similar amounts of total syntrophin, as judged by immunoblotting (pan-Syn, mAb SYN1351). A duplicate blot was probed with mAb Mandys-8 (Dys), stripped, and reprobed with mAb DRP-1 (Utr). Positions of molecular mass markers (in kD) are shown in some panels. These results were replicated twice, and representative blots from a single experiment are shown.