The reconstruction of myosin filaments in rabbit psoas muscle from solubilized myosin

1986 ◽  
Vol 7 (2) ◽  
pp. 97-109 ◽  
Author(s):  
Maria C. Maw ◽  
Arthur J. Rowe
Keyword(s):  
Psoas Muscle ◽  
Rabbit Psoas ◽  
Myosin Filaments

scholarly journals Quantitative studies on the polarization optical properties of striated muscle. I. Birefringence changes of rabbit psoas muscle in the transition from rigor to relaxed state.

1976 ◽  
Vol 68 (3) ◽  
pp. 497-511 ◽  
Author(s):  
D L Toylor
Keyword(s):  
Striated Muscle ◽  
Polarized Light ◽  
Psoas Muscle ◽  
Maximum Increase ◽  
Rabbit Psoas ◽  
Form Birefringence ◽  
Quantitative Studies ◽  
Relaxation Solution ◽  
Myosin Filaments ◽  
Rigor Solution

The changes in birefringence in the rigor to relax transition of single triton-extracted rabbit psoas muscle fibers have been investigated with quantitative polarized light techniques. The total birefringence of rest lenght fibers in rigor was (1.46 +/- 0.08) x 10(-3) and increased to (1.67 +/- 0.05) x 10(-3) after Mg-ATP relaxation. Pyrophosphate relaxation increased the total birefringence only slightly, whereas subsequent Mg-ATP relaxation elicited the maximum increase in birefringence. Changes in lattice spacing did not account for the total increase in birefrigence during relaxation. Moreover, the increase in total birefringence was attributable to increases in intrinsic birefringence as well as form birefringence. No change in birefringence was exhibited upon exposure to a relaxation solution after myosin extraction. Synthetic myosin filaments were prepared and treated with relaxation and rigor solutions. The negatively stained filaments treated with a rigor solution had gross irregular projections at either end, while the filaments treated with a relaxing solution were more spindle shaped. The results are compatible with the view that the subfragment-2 moieties of myosin angle away from the myosin aggregates (light meromyosin) to permit the attachment of the subfragment-1 moieties to actin.

scholarly journals Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line.

1988 ◽  
Vol 107 (6) ◽  
pp. 2199-2212 ◽  
Author(s):  
K Wang ◽  
J Wright
Keyword(s):  
Skeletal Muscle ◽  
Skeletal Muscles ◽  
Smooth Muscles ◽  
Psoas Muscle ◽  
Immunoblot Analysis ◽  
Cross Reactivity ◽  
Wide Range ◽  
Determining Factors ◽  
Myosin Filaments ◽  
In Series

Nebulin, a giant myofibrillar protein (600-800 kD) that is abundant (3%) in the sarcomere of a wide range of skeletal muscles, has been proposed as a component of a cytoskeletal matrix that coexists with actin and myosin filaments within the sarcomere. Immunoblot analysis indicates that although polypeptides of similar size are present in cardiac and smooth muscles at low abundance, those proteins show no immunological cross-reactivity with skeletal muscle nebulin. Gel analysis reveals that nebulins in various skeletal muscles of rabbit belong to at least two classes of size variants. A monospecific antibody has been used to localize nebulin by immunoelectron microscopy in a mechanically split rabbit psoas muscle fiber preparation. Labeled split fibers exhibit six pairs of stripes of antibody-imparted transverse densities spaced at 0.1-1.0 micron from the Z line within each sarcomere. These epitopes maintain a fixed distance to the Z line irrespective of sarcomere length and do not exhibit the characteristic elastic stretch-response of titin epitopes within the I band domain. It is proposed that nebulin constitutes a set of inextensible filaments attached at one end to the Z line and that nebulin filaments are in parallel, and not in series, with titin filaments. Thus the skeletal muscle sarcomere may have two sets of nonactomyosin filaments: a set of I segment-linked nebulin filaments and a set of A segment-linked titin filaments. This four-filament sarcomere model raises the possibility that nebulin and titin might act as organizing templates and length-determining factors for actin and myosin respectively.

scholarly journals Differences in the Charge Distribution of Glycerol-Extracted Muscle Fibers in Rigor, Relaxation, and Contraction

1974 ◽  
Vol 64 (5) ◽  
pp. 551-567 ◽  
Author(s):  
Suzanne M. Pemrick ◽  
Charles Edwards
Keyword(s):  
Charge Distribution ◽  
Sarcomere Length ◽  
Muscle Fibers ◽  
Psoas Muscle ◽  
Nonlinear Relationship ◽  
Thin Filaments ◽  
Rabbit Psoas ◽  
Relaxation Solution ◽  
The Difference ◽  
Rest Length

Glycerol-extracted rabbit psoas muscle fibers were impaled with KCl-filled glass microelectrodes. For fibers at rest-length, the potentials were significantly more negative in solutions producing relaxation than in solutions producing either rigor or contraction; further the potentials in the latter two cases were not significantly different. For stretched fibers, with no overlap between thick and thin filaments, the potentials did not differ in the rigor, the relaxation, or the contraction solutions. The potentials measured from fibers in rigor did not vary significantly with the sarcomere length. For relaxed fibers, however, the potential magnitude decreased with increasing sarcomere length. The difference between the potentials measured for rigor and relaxed fibers exhibited a nonlinear relationship with sarcomere length. The potentials from calcium-insensitive fibers were less negative in both the rigor and the relaxation solutions than those from normal fibers. When calcium-insensitive fibers had been incubated in Hasselbach and Schneider's solution plus MgCl2 or Guba-Straub's solution plus MgATP the potentials recorded upon impalement were similar in the rigor and the relaxation solution to those obtained from normal fibers in the relaxed state. It is concluded that the increase in the negative potential as the glycerinated fiber goes from rigor to relaxation may be due to an alteration in the conformation of the contractile proteins in the relaxed state.

scholarly journals ANOMALOUS CONTRACTION OF INVERTEBRATE STRIATED MUSCLE

1965 ◽  
Vol 27 (3) ◽  
pp. 639-649 ◽  
Author(s):  
R. E. Stephens
Keyword(s):  
Mass Distribution ◽  
Striated Muscle ◽  
Psoas Muscle ◽  
Homarus Americanus ◽  
Limulus Polyphemus ◽  
Polarization Microscopy ◽  
Trypsin Treatment ◽  
Rabbit Psoas ◽  
Ultraviolet Microbeam ◽  
Intrinsic Birefringence

The phenomenon of A band shortening or contraction has been investigated in glycerinated myofibrils of Pecten irradians, Homarus americanus, Cambarus virilis, and Limulus polyphemus through the techniques of ultraviolet microbeam inactivation and polarization microscopy. With the former method, it has been shown that these muscles, even though exhibiting the shortening effect, contract in a manner consistent with only the sliding filament model. Intrinsic birefringence studies have indicated no significant changes in mass distribution or orientation within the shortened A bands. Except in the case of Limulus muscle, the shortening effect was seen only in contraction under tension. The magnitude of this anomalous phenomenon was dependent upon glycerination time and has been duplicated in rabbit psoas muscle through brief trypsin treatment. A band shortening could not be observed in glutaraldehyde-fixed muscle or in myofibrils glycerinated for only short periods. It has been concluded that the phenomenon of A band contraction is an artifact induced by the glycerination procedure, possibly through weakening of the sarcomere structure. However, the fact that the A band shortens under tension rather than lengthens poses an interesting paradox.

scholarly journals Tropomyosin is in a reduced state in rabbit psoas muscle

2011 ◽  
Vol 32 (1) ◽  
pp. 19-21 ◽  
Author(s):  
Sherwin S. Lehrer ◽  
Socheata Ly ◽  
Franklin Fuchs
Keyword(s):  
Psoas Muscle ◽  
Rabbit Psoas ◽  
Reduced State
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