Relationship among fibre type, myosin ATPase activity and contractile properties
dc.contributor.author | Maxwell, Leo C. | en_US |
dc.contributor.author | Faulkner, John A. | en_US |
dc.contributor.author | Murphy, Richard A. | en_US |
dc.date.accessioned | 2006-09-08T20:47:35Z | |
dc.date.available | 2006-09-08T20:47:35Z | |
dc.date.issued | 1982-11 | en_US |
dc.identifier.citation | Maxwell, Leo C.; Faulkner, John A.; Murphy, Richard A.; (1982). "Relationship among fibre type, myosin ATPase activity and contractile properties." The Histochemical Journal 14(6): 981-997. <http://hdl.handle.net/2027.42/42851> | en_US |
dc.identifier.issn | 0018-2214 | en_US |
dc.identifier.issn | 1573-6865 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/42851 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6217171&dopt=citation | en_US |
dc.description.abstract | At least two types of skeletal muscle myosin have been described which differ in ATPase activity and stability in alkaline or acidic media. Differences in ATPase characteristics distinguish Type I and Type II fibres histochemically. In this study, ATPase activity of myosin from muscles of several species with known histochemical and contractile properties has been determined to test the hypothesis that (1) myosin ATPase activity, (2) histochemical determination of fibre types and (3) maximum shortening velocity, all provide equivalent estimates of contractile properties in muscles of mixed fibre types. Maximum shortening velocity appears to be proportional to ATPase activity as expected from previous reports by Barany. However, both myosin ATPase and the maximum shortening velocity exhibit curvilinear relationships to the fraction of cross-sectional area occupied by Type II fibres. Therefore, we reject the hypothesis and conclude that histochemically determined myofibrillar ATPase does not accurately reflect the intrinsic ATPase activity or shortening velocity in muscles of mixed fibre types. Our data are consistent with the presence of more than two myosin isozymes or with a mixture of isozymes within single muscle fibres. | en_US |
dc.format.extent | 1049701 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers; Chapman and Hall Ltd ; Springer Science+Business Media | en_US |
dc.subject.other | Life Sciences | en_US |
dc.subject.other | Biomedicine General | en_US |
dc.subject.other | Cell Biology | en_US |
dc.subject.other | Animal Anatomy / Morphology / Histology | en_US |
dc.subject.other | Biological Microscopy | en_US |
dc.title | Relationship among fibre type, myosin ATPase activity and contractile properties | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Physiology, The University of Michigan, 48109, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationother | Department of Physiology, The University of Texas Health Science Center, 78284, San Antonio, Texas, USA | en_US |
dc.contributor.affiliationother | Department of Physiology, The University of Virginia, 22901, Charlottesville, Virginia, USA | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 6217171 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/42851/1/10735_2005_Article_BF01005238.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/BF01005238 | en_US |
dc.identifier.source | The Histochemical Journal | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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