SUMMARY –Changes occurring during stretching and post‐mortem aging of intramuscular collagen from bovine muscle were studied. Sucrose density‐gradient ultracentrifugation analyses of denatured guanidine hydrochloride‐soluble intramuscular collagen (GSIC) indicated stretching and/or aging muscle changes the molecular structure of the collagen. The quantity of aldehyde cross‐links in native GSIC supported this finding. The yield of GSIC from stretched muscles was slightly greater than from normal muscles. A high correlation existed between quantity of each collagen chain component and muscle shear value. Stretched muscle had significantly longer sarcomeres than normal muscles, regardless of aging period. Sarcomere length and muscle tenderness were closely associated in unaged muscle.
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KRUGGEL et al. (1971) studied this question.
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