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Studies on the Rigor Resulting from the Thawing of Frozen Frog Sartorius Muscle

Overview
Journal J Gen Physiol
Specialty Physiology
Date 1950 May 20
PMID 15422110
Citations 2
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Abstract

1. The rigor which takes place when completely frozen frog sartorius muscle is thawed ("thaw rigor"), is accompanied by a decrease in length of 70 per cent and a loss in weight of 35 per cent, whether the muscle is frozen in the resting or the exhausted condition, or during isometric tetanus. Muscle tetanized to maximal shortening shows a loss in weight of 25 per cent on thawing. 2. A load of 8 gm. is sufficient to prevent the decrease in length on thawing, but after its removal the muscle will shorten almost to the normal extent. 3. Inhibitors such as azide, cyanide, 2:4 dinitrophenol, p-chloromercuribenzoate, Cu, and hydrogen peroxide, when used for periods not exceeding 1 hour, have little effect on the shortening; although in some cases these poisons render the muscle inexcitable. 4. Muscles poisoned with iodoacetic acid and stimulated to exhaustion, or maintained at fixed length in nitrogen, show little or no shortening on thawing. ATP can produce shortening in the muscles in which it has been prevented. 5. The phenomenon is considered to be due to an in situ synaeresis of the actomyosin of the myofibrils. As a result of the disorganisation of the muscle protoplasm produced by the freezing and subsequent thawing, the ATP, which must be bound or localized in the resting muscle, can act on the myofibril in a similar manner to its in vitro effect on the actomyosin thread.

Citing Articles

The adenosinetriphosphatase activity of myofibrils isolated from skeletal muscle.

PERRY S Biochem J. 1951; 48(3):257-65.

PMID: 14820852 PMC: 1275307. DOI: 10.1042/bj0480257.


Water loss during contracture of muscle.

KAMINER B J Gen Physiol. 1962; 46:131-42.

PMID: 14453453 PMC: 2195250. DOI: 10.1085/jgp.46.1.131.

References
1.
Needham D . The adenosinetriphosphatase activity of myosin preparations. Biochem J. 1942; 36(1-2):113-20. PMC: 1265669. DOI: 10.1042/bj0360113. View

2.
Bailey K . Myosin and adenosinetriphosphatase. Biochem J. 1942; 36(1-2):121-39. PMC: 1265670. DOI: 10.1042/bj0360121. View

3.
Dubuisson M . Appearance of a new protein, contractin, in extracts of contracted muscles. Experientia. 1948; 4(11):437-40. DOI: 10.1007/BF02145000. View

4.
Cross R, TAGGART J . Studies on the cyclophorase system; the coupling of oxidation and phosphorylation. J Biol Chem. 1949; 177(2):655-78. View

5.
BORBIRO M, SZENT-GYORGYI A . On the relation between tension and adenosine triphosphate in cross-striated muscle. Biol Bull. 1949; 96(2):162-7. View