Ultrastructure of skeletal muscle fibers studied by a plunge quick freezing method

Myofilament lengths

Hernando J. Sosa, D. Popp, G. Ouyang, H. E. Huxley

Research output: Contribution to journalArticle

85 Citations (Scopus)

Abstract

We have set up a system to rapidly freeze muscle fibers during contraction to investigate by electron microscopy the ultrastructure of active muscles. Glycerinated fiber bundles of rabbit psoas muscles were frozen in conditions of rigor, relaxation, isometric contraction, and active shortening. Freezing was carried out by plunging the bundles into liquid ethane. The frozen bundles were then freeze-substituted, plastic-embedded, and sectioned for electron microscopic observation. X-ray diffraction patterns of the embedded bundles and optical diffraction patterns of the micrographs resemble the x- ray diffraction patterns of unfixed muscles, showing the ability of the method to preserve the muscle ultrastructure. In the optical diffraction patterns layer lines up to 1/5.9 nm-1 were observed. Using this method we have investigated the myofilament lengths and concluded that there are no major changes in length in either the actin or the myosin filaments under any of the conditions explored.

Original languageEnglish (US)
Pages (from-to)283-292
Number of pages10
JournalBiophysical Journal
Volume67
Issue number1
StatePublished - 1994
Externally publishedYes

Fingerprint

Myofibrils
Skeletal Muscle Fibers
Freezing
Muscles
Psoas Muscles
Ethane
Isometric Contraction
Myosins
X-Ray Diffraction
Plastics
Actins
Electron Microscopy
X-Rays
Electrons
Rabbits

ASJC Scopus subject areas

  • Biophysics

Cite this

Ultrastructure of skeletal muscle fibers studied by a plunge quick freezing method : Myofilament lengths. / Sosa, Hernando J.; Popp, D.; Ouyang, G.; Huxley, H. E.

In: Biophysical Journal, Vol. 67, No. 1, 1994, p. 283-292.

Research output: Contribution to journalArticle

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