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. 2004 May 24;165(4):505–515. doi: 10.1083/jcb.200307164

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Copyright © 2004, The Rockefeller University Press

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Figure 3. — MALDI-TOF mass spectrometry analysis of MuSK complex isolated from Torpedo AChR-rich membranes. (A) Cross-linking experiment showing a major 140-kD MuSK cross-linked product in Torpedo AChR-rich membranes. After separation on SDS-PAGE, MuSK (97 kD) from control membranes (left lane) and from cross-linked membranes (right lane, +SMPB) were revealed by Western-blotting using anti-MuSK antibodies (Abs 2847). (B) Immunoprecipitation experiments performed on Triton X-100 extracts from uncross-linked Torpedo postsynaptic membranes with anti-MuSK antibodies. Lane 1 shows the presence of two polypeptides of relative MW 97 and 40 kD (silver staining after SDS-PAGE). Lane 2 shows Western blots performed with anti-MuSK showing that the 97-kD polypeptide corresponds to MuSK. (C) MALDI-TOF mass spectrometry analysis of the 140-kD cross-link product and the 40-kD polypeptide. Coverage maps are shown. Coverages of 6% with rat MuSK (top) and of 14% with rat AChE-associated collagen (ColQ) were obtained from the 140-kD cross-link product. On the 19 experimental tryptic peptides identified, seven matched with rat ColQ (182-190, 282-292, 158-169, 170-181, 155-169, 158-175, and 314-332). The matched peptides represent 79/458 residues of ColQ (14%). For the 40-kD polypeptide, a coverage of 20% was found with rat AChE-associated collagen. On the 15 experimental tryptic peptides identified, seven matched with rat ColQ (185-196, 200-211, 188-199, 155-169, 314-332, 197-217, and 238-261). The matched peptides represent 106/458 residues of ColQ (20%).