Abstract:
:Electron microscopy of mammalian smooth muscle myosin rods showed them to be 153 +/- 7 nm (SD) long, and to bend sharply (greater than 90 degrees) but infrequently, and pH independently (range 6.5-9.5), at a single site 45 +/- 4 nm from one end of the molecule. Light meromyosin (LMM) preparations were 99 +/- 10 nm long, and showed no bends. Intrinsic viscosity vs temperature plots for rods and LMM indicated that neither fragment changed in flexibility in the range 4-40 degrees C. Peptide mapping in the presence and absence of SDS established that the proteolytic susceptibility of the hinge at the N terminus of LMM reflects the presence of locally different structure, and not simply a clustering of susceptible residues. The isolated smooth muscle myosin rod thus contains only a single hinge, having significant stiffness, and lacks the second bend seen under certain conditions in the intact molecule.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Cross RAdoi
10.1016/0014-5793(84)80940-0subject
Has Abstractpub_date
1984-10-15 00:00:00pages
197-201issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(84)80940-0journal_volume
176pub_type
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