36.
Myosin was isolated from two types of muscle, ordinary and dark muscles, of three species of fish living in sea water. The
compositions of light chains were visualized by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and the
mechanochemical activity was examined by
in vitro motility and ATPase assays. Ordinary muscle myosin of either species had three species of light chain, whereas dark muscle
myosin had another two species of light chain judged by SDS-PAGE. Sliding velocity of ordinary muscle myosin was in the range
of 4.92–6.89 μm/S, whereas that of dark muscle myosin was in the range of 3.07–4.25 μm/s. Therefore, ordinary muscle myosin
showed 1.26–1.95 times higher sliding velocity than dark muscle myosin in either species. The ratios of V
max of actin-activated Mg
2+-ATPase activity of ordinary to dark muscle myosins were correlated quite well to the ratios of sliding velocity. Activity
of ordinary muscle myosin was comparable to that of mammalian fast muscle myosin, but that of dark muscle myosin was twice
of that of mammalian slow muscle myosin. These results may reflect the essential role of fish dark muscle myosin always used
in slow cruising.
相似文献