S. Watabe et al., CARP EXPRESS SPECIFIC ISOFORMS OF THE MYOSIN CROSS-BRIDGE HEAD, SUBFRAGMENT-1, IN ASSOCIATION WITH COLD AND WARM TEMPERATURE-ACCLIMATION, Journal of thermal biology, 19(4), 1994, pp. 261-268
1. The 81 fragment is the head of the myosin cross-bridge which is the
force generator for muscle contraction and has actin binding and ATPa
se sites. The latter is believed to determine the rate of myosin cross
-bridge cycling and hence power production by the muscle fibres. 2. Po
lyacrylamide gel electrophoresis in the presence of sodium pyrophospha
te (PPi-PAGE) showed that carp acclimated to 10 degrees C contained fo
ur isoforms of chymotryptic myosin Sl in fast skeletal muscle. Peptide
mapping revealed that these consisted of two types of S1 heavy chain,
H1 and H2, with different primary structures. Four S1 isoforms in tot
al, H1 (A1), H1 (A2), H2 (A1), and H2 (A2), were separated in PPi-PAGE
with two associated light chains, A1 and A2. 3. Fish acclimated to 30
degrees C contained another type of S1 heavy chain, H3, and thus incl
uded two S1 isoforms, H3 (A1) and H3 (A2). 4. These results suggest a
possible genetic regulation for different S1 isoform expression in an
acclimation temperature-dependent manner.