Abstract：
:The myosin-containing A-filaments of vertebrate skeletal muscle contain 294 myosin molecules packed to give overall 3-fold rotational symmetry, as illustrated by the fraying of the filament into 3 sub-filaments ( Maw and Rowe, 1980). Further studies on slightly frayed filaments are consistent with a highly linear arrangement of these sub-filaments, at least in the major part of the cross-bridge region where sub-filaments can be observed. Isolated filaments have an unusual hydrodynamic property in the form of an anomalous frictional increment. This property is as yet unexplained; it may possibly be related to flow-induced cyclic movements in the myosin heads. Self-assembly of A-filaments in vitro to correct length and width has yet to be achieved. We have found however that under certain exactly defined conditions a very accurate reconstruction of both filaments and A-band can be accomplished in situ. Solubilisation of the myosin in chloride-free medium and maintenance of a high local myosin concentration are absolute requirements. Reconstruction is either abolished or modified by preglycerolation or at longer sarcomere length. It is argued that these results suggest a role for the actin filament lattice in myosin assembly, and imply that myosin assembly in the M-line region may be separable from myosin assembly in the cross-bridge region.
journal_name
Adv Exp Med Bioljournal_title
Advances in experimental medicine and biologyauthors
Rowe AJ,Maw MCdoi
10.1007/978-1-4684-4703-3_2subject
Has Abstractpub_date
1984-01-01 00:00:00pages
5-20eissn
0065-2598issn
2214-8019journal_volume
170pub_type
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