Preparation of heavy meromyosin from the autolyzed squid [Todarodes pacificus] mantle muscle homogenate

Incubation of squid mantle muscle homogenate caused a selective cleavage of myosin into heavy meromyosin (HMM) and light meromyosin (LMM). HMM was isolated from the incubated homogenate by using ammonium sulfate fractionation. The purified HMM retained two types of light chain components. Its Mg2+-ATPase activity with or without F-actin showed a Ca-sensitivity. HMM was cleaved into subfragment-1 and subfragment-2 upon chymotryptic digestion with or without Ca2+, possessing different light chain composition. Two types of light chain component were kept intact when digested in the presence of Ca2+. Ca2+ stabilized HMM especially in a bound form to F-actin.