Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-6-24
pubmed:abstractText
The position of the large troponin complex relative to myosin crossbridges in Lethocerus flight muscle (IFM) has been probed by electron microscopy (EM) using monoclonal antibodies against troponin T (TnT) and troponin H (TnH), a heavy troponin component found in several insect muscles. Infiltration of gold-tagged and plain Fab fragments into glycerinated IFM before fixation established in non-overlap fibers that the beads every 38.7 nm along thin filaments are troponin. Original and optically filtered EM images from 25 nm longitudinal and 15 nm cross-sections of partially overlapped fibers suggests that epitopes on both TnT and TnH are very close to the rear crossbridge of the rigor double chevron. When Fab was infiltrated into relaxed fibers and ATP was subsequently removed, the resulting rigor crossbridge lattice was disrupted by antibody labeling of the troponin. The results confirm that the lattice of rigor crossbridges and troponin are congruent and suggest that crossbridges may interact with troponin in IFM, possibly serving as a partial basis for the stretch activation characteristic of this muscle.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
239
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
52-67
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Gold/Fab immuno electron microscopy localization of troponin H and troponin T in Lethocerus flight muscle.
pubmed:affiliation
Department of Cell Biology, Duke University Medical Center, Durham, NC 27710.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't