[Chemical suturing of myosin and actin to capron fiber]

Immobilization of myosin, actin, actomyosin and subfragment S1 on kapron fibre was achieved with the help of glutaric aldehyde. The ATPase activity of myosin and its ability to interact with actin is preserved; while the ATPase activity of S1 subfragment decreases considerably. The immobilization on kapron fibre changes the pH-dependance of ATPase activity of myosin and that of subfragment S1, shifting the maximum to low pH zone (pH 5.5), and increases the thermostability of the enzyme. The ions of Ca++ in all cases act as an activating agent on ATPase while the ions of Mg++ either do not affect myosin and subfragment S1 at all, or increase the activity in the case of the immobilized of actomyosin but to a lesser degree than the ions of Ca++. The immobilized actin preserves its ability to form actomyosin complex.