The study demonstrates that Mg2+ ADP binding to myofibrils is similar to actomyosin-subfragment one, reflecting constraints on myosin cross-bridges imposed by the regular array of thick and thin filaments.
Myofibrillar data extend subfragment models via filament constraints; leaves open relevance to human cardiac mechanics.
The binding of Mg2+ ADP to both rabbit skeletal and bovine cardiac myofibrils has been studied at two different temperatures. In each case a single class of binding sites was observed with a binding constant very close to that reported for the analogous actomyosin-subfragment one but much weaker than that seen with the analogous myosin subfragment one alone. These findings are discussed in terms of the constraints on the myosin cross-bridges imposed by the regular array of thick and thin filaments found in myofibrils.
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Johnson et al. (1984) studied this question.
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