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. 1967 Aug 1;34(2):431–445. doi: 10.1083/jcb.34.2.431

MORPHOLOGY OF RIGOR-SHORTENED BOVINE MUSCLE AND THE EFFECT OF TRYPSIN ON PRE- AND POSTRIGOR MYOFIBRILS

Marvin H Stromer 1, D E Goll 1, L E Roth 1
PMCID: PMC2107327  PMID: 5340759

Abstract

Bovine semitendinosus muscles were sampled immediately after death, after 24 hr postmortem with storage at 2°, 16°, or 37°C, and after 312 hr postmortem with storage at 2° and 16°C. A biopsy technique was used to prevent shortening during glutaraldehyde fixation. Postfixation in osmium tetroxide was followed by embedding in an Epon-Araldite mixture. Bovine muscle was supercontracted after 24 hr storage at 27deg; but was only slightly contracted after storage at 16° for 24 hr. Muscle held at 37° for 24 hr was slightly less supercontracted than the 2° muscle. Striking similarities existed between muscles stored at 16° and at 2°C for 312 hr. Both were slightly shortened with narrowed I bands and an area of increased density, probably due to overlap of thin filaments in the middle of the A band. Postmortem shortening was accompanied by banding-pattern changes similar to those predicted for contracting muscle by Huxley and Hanson's sliding filament model. Treatment of myofibrils with 0.05% trypsin resulted in a rapid loss of Z lines and, in supercontracted myofibrils, caused a return of the banding pattern of resting muscle.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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