Fig. 1
Comparisons of protein contents of MHC-isoforms, αB-crystallin and α-tubulin in a variety of rat striated muscles. a Immunoblotting bands showing αB-crystallin, α-tubulin, and HSC 70 (control). Numbers labeled under the figure represent respective striated muscles; atrium (1), ventricle (2), masseter (3), tongue (4), diaphragm (5), soleus (6), plantaris (7), gastrocnemius (8), extensor digitorum longus (9), tibialis anterior (10), and psoas (11) muscles. Protein quantities per lane were 1.6, 50, and 20 μg for αB-crystallin, α-tubulin, and HSC 70, respectively. b Immunoblotting bands showing α-tubulin corresponding to the same striated muscles as in a. Protein quantities of total muscle extracts loaded per lane were lane 1 8 μg, lane 2 8 μg, lane 3 30 μg, lane 4 13 μg, lane 5 15 μg, lane 6 8 μg, lane 7 28 μg, lane 8 25 μg, lane 9 25 μg, lane 10 40 μg, lane 11 50 μg. c Typical SDS-PAGE pattern showing MHC-isoform composition. IIa, IId, IIb, α, and I indicate MHC-IIa, MHC-IId, MHC-IIb, α-MHC, and MHC-I, respectively. Attached numbers are the same as in a. Protein loaded for each lane was 1.6 μg