Rj. Talmadge et Rr. Roy, ELECTROPHORETIC SEPARATION OF RAT SKELETAL-MUSCLE MYOSIN HEAVY-CHAIN ISOFORMS, Journal of applied physiology, 75(5), 1993, pp. 2337-2340
A new technique for the sodium dodecyl sulfate-polyacrylamide gel elec
trophoretic separation of rat skeletal muscle myosin heavy-chain (MHC)
isoforms is presented. This technique allows for the separation of th
e four identified MHC isoforms known to be present in adult rat skelet
al muscle. These types of MHC are commonly called I, IIa, IIx or IId,
and IIb. The procedure can be performed using minigel electrophoresis
systems and does not involve preparation of gradient-separating gels o
r the use of special cooling devices. The procedure accommodates both
silver and Coomasie Blue staining. Thus the procedure is simple to per
form and highly repeatable, providing high-resolution separation of MH
C protein isoforms. The percent composition of the four adult MHCs in
rat soleus, medial gastrocnemius, diaphragm, and levator ani muscles b
y use of this procedure and Coomasie Blue staining is similar to that
previously reported. This new technique provides a novel and easy-to-p
erform method for the separation of rat skeletal muscle MHC isoforms.