The study determined the 127-amino-acid sequence of the hinge region in adult chicken pectoralis muscle myosin, revealing high sequence identity with rabbit cardiac muscle alpha-myosin.
Preclinical avian myosin sequence data; leaves open comparative functional studies on cardiac isoforms without clinical implications.
The CNBr fragments of the hinge region in the carboxyterminal portion of long subfragment-2 derived from adult chicken pectoralis muscle myosin were isolated and sequenced by conventional methods. The alignment of these fragments was deduced from the homology of their sequences with those of other myosins, so that the sequence of the hinge region consisting of 127 amino-acid residues was determined. A comparison of this sequence with that of chicken embryonic skeletal muscle, chicken gizzard muscle and rabbit cardiac muscle (alpha-myosin) shows degrees of 95%, 36% and 82% sequence identities, respectively. Furthermore, the frequency with which hydrophobic residues are present at position "a" in seven-residues repeats of this region was significantly lower than the other portions of the rod.
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Bunji Watanabe (1989) studied this question.
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