Tryptic digestion of myosin S-1 in the presence of ATP reduces its thermal stability due to cleavage of the 25 kDa amino-terminal fragment.
No immediate clinical implications; leaves open whether this cleavage modulates cardiac myosin function in vivo.
Myosin subfragment-1 (S-1), digested with trypsin in the presence of ATP, rapidly loses its ATPase activity upon mild heat treatment even if ATP or ADP is present. The heat-treated molecule is very sensitive to further tryptic digestion. Undigested S-1 and S-1 digested in the absence of ATP are protected by nucleotides. The loss of the protective effect of nucleotides correlates with the tryptic splitting of the 25 kDa amino-terminal fragment between Arg 23 and Ile 24.
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Pintér et al. (1986) studied this question.
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