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Journal of Animal Science, Vol 70, Issue 3 798-804, Copyright © 1992 by American Society of Animal Science
JOURNAL ARTICLE |
G. Whipple and M. Koohmaraie
Roman L. Hruska U.S. Meat Animal Research Center, ARS, U.S. Department of Agriculture, Clay Center, NE 68933.
The objectives of this study were to examine the amount of postmortem proteolysis in three different lamb muscles at different ages and to determine whether a relationship exists between the extent of myofibrillar degradation and certain endogenous proteinase activities. Wether lambs were slaughtered at 8 (n = 6) and 26 (n = 6) wk of age. Samples were taken from the longissimus (LM), gluteus medius (GM), and supraspinatus (SS) muscles for determining myofibrillar fragmentation index (MFI) at 1 and 7 d postmortem, cathepsins B and B + L, cystatin(s), mu- and m-calpain and calpastatin 24-h activities, and muscle fiber type and area. Muscle samples were removed for SDS-PAGE analysis at 0, 1, and 7 d postmortem. The SS muscle consisted of more (P less than .05) oxidative fibers, whereas no age effects (P greater than .10) were observed for fiber type. The younger lambs had higher (P less than .01) cathepsins B and B + L, cystatin, and calpastatin 24-h activities but less (P less than .01) m-calpain activity than did the 26-wk-old lambs. Within each age, the SS muscle had the highest (P less than .05) mu-calpain, m-calpain, and calpastatin specific activities. The MFI values and SDS-PAGE results indicate that less proteolysis occurred in the SS muscle. Samples from 26-wk-old lambs tended to have greater MFI values at 1 and 7 d postmortem, especially for the LM and GM muscles. From these results, it seems that less postmortem proteolysis occurs in younger and more oxidative muscles and this may be attributed to the greater calpastatin 24-h activity.
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