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1.
Meat tenderness is considered as the most important criterion for meat quality by consumers and can be improved by the actions of endogenous proteases, mainly calpains, during postmortem storage at 0–5°C. The purpose of this study, therefore, was to examine the postmortem calpain activation and proteolysis in breast (BM) and leg and thigh (LM) muscles of White Roman goose. BM and LM were taken from goose carcasses (n = 15) at 0 (10–15 min postmortem), 1, 3, and 7 days of storage at 5°C. The decrease in postmortem pH, calpain‐1 and ‐11 activities, and contents of the calpain‐1 80 kDa subunit and desmin was more rapid (p < .05) in BM than in LM. Our results show that postmortem proteolysis was more extensive in BM than in LM of White Roman goose, not only because the difference in fiber type composition between two muscles, but because the rate and extent of calpain activation were greater in BM as well. These results may provide useful information to optimize meat processing for different muscles in goose industry.  相似文献   

2.
This study assessed the influence of stewing (1, 2 or 3 h) on the texture, ultrastructure and in vitro digestibility of meat from the yellow‐feathered chicken, which is a popular broiler chicken in Asia. Results indicated that longer stewing considerably increased cooking loss of the chicken carcass and tenderness of thigh meat. After 3 h of stewing, protein digestibility decreased from 90.5% to 80.3% and fiber diameter decreased by 8.63 μm. The shear force value of breast meat decreased from 32.34 N at 1 h to 10.29 N at 2 h, and then increased to 39.98 N at 3 h. The texture profile of breast meat remarkably decreased during stewing. Moreover, increased stewing time induced longitudinal and transversal shrinkage of muscle fibers and the degradation of the myosin heavy chain. These findings suggested that prolonged stewing (3 h) resulted in decreased meat qualities, based on the changes in cooking loss, digestibility and texture profile, but that stewing for 2 h increased thigh and breast tenderness. Producers could utilize this information to stew yellow‐feathered chicken meat with desirable qualities.  相似文献   

3.
钙蛋白酶系统在肌肉生长和肉品嫩化方面的研究   总被引：1，自引：0，他引：1  
钙蛋白酶系统主要由钙蛋白酶(calpain)及钙蛋白酶抑制蛋白(calpastatin)组成,calpain是存在于细胞质中的依赖于Ca2+的中性蛋白酶,calpastatin是钙蛋白酶的内源抑制蛋白。近年的研究表明,calpain是细胞质中主要的蛋白水解酶,在肌原纤维蛋白降解中起着重要的作用。肌肉增长和宰后嫩度的变化与蛋白质水解程度密切相关。因此,钙蛋白酶系统的活性会影响畜禽肌肉增长和肉的嫩度。文中综述了钙蛋白酶系统各种酶的结构及其如何在肌肉生长和肉的嫩化中起作用。  相似文献   

4.
Calpain 3/p94 is not involved in postmortem proteolysis   总被引：1，自引：0，他引：1  
Studies on the correlation between expression and/or autolysis of calpain and postmortem proteolysis in muscle have provided conflicting evidence regarding the possible role of calpain 3 in postmortem tenderization of meat. Thus, the objective of this research was to test the effect of postmortem storage on proteolysis and structural changes in muscle from normal and calpain 3 knockout mice. Knockout mice (n = 6) were sacrificed along with control mice (n = 6). Hind limbs were removed and stored at 4 degrees C; muscles were dissected at 0, 1, and 3 d postmortem and subsequently analyzed individually for degradation of desmin. Pooled samples for each storage time and mouse type were analyzed for degradation of nebulin, dystrophin, vinculin, and troponin-T. In a separate experiment, hind-limb muscles from knockout (n = 4) and control mice (n = 4) were analyzed for structural changes at 0 and 7 d postmortem using light microscopy. As an index of structural changes, fiber detachment, cracked or broken fibers, and the appearance of space between sarcomeres were quantified. Cumulatively, the results of the first experiment indicated that postmortem proteolysis of muscle occurred similarly in control and in calpain 3 knockout mice. Desmin degradation did not differ (P > 0.99), and there were no indications that degradation of nebulin, dystrophin, vinculin, and troponin-T were affected by the absence of calpain 3 in postmortem muscle. Structural changes were affected by time postmortem (P < 0.05), but not by the absence of calpain 3 from the muscles. In conclusion, these results indicate that calpain 3 plays a minor role, if any, in postmortem proteolysis in muscle.  相似文献   

5.
The objective of this study was to investigate changes occurring in μ/m‐calpain in post mortem chicken muscles and to determine the origin of the unknown bands found in calpain casein zymography. The unknown bands were reported with slightly greater mobility compared to conventional μ/m‐calpain bands in casein zymography. Identification of these bands was accomplished using native polyacrylamide gel electrophoresis, liquid chromatography tandem mass spectrometry and with protein phosphatase treatment. Results showed that the unknown bands were corresponding to μ/m‐calpain, and dephosphorylation by protein phosphatase did not change their appearance. The calpain samples were then incubated with various concentrations of Ca2+ to determine the relationship between changes in μ/m‐calpain and the appearance of the unknown bands. The products of μ/m‐calpain partial autolysis were found to be consistent with the appearance of the unknown bands. Therefore, the appearance of these bands did not result from phosphorylation of μ/m‐calpain as previously hypothesized, but from partial autolysis of μ/m‐calpain. Also their presence suggests that μ/m‐calpain undergoes partial autolysis during aging which may play certain roles in meat quality improvement.  相似文献   

6.
The present experiment was conducted to determine the effect of muscle temperature during the prerigor and early postrigor period on meat tenderness, postmortem proteolysis, calpain system activity, water-holding capacity, and color. Lamb longissimus muscle (n = 14) from the right and left carcass sides was excised immediately after dressing, divided into an anterior and posterior sample, vacuum-packaged, and stored overnight at 5 to 35 degrees C. Further storage, up to 14 d postmortem, was at 2 degrees C. Tenderness at 1 d postmortem, tenderization during further storage, and postmortem proteolysis were negatively affected by overnight incubation above 25 degrees C. This effect could be explained by an effect of temperature on muscle contraction and activity of the calpain system. Muscle contraction was at a minimum after incubation at 15 degrees C. Water-holding capacity was negatively affected by incubation above 25 degrees C. Color scores improved with increasing incubation temperature at 1 d postmortem. However, after 14 d of postmortem storage, no differences in color scores were observed. Based on the present results and results of other groups, a temperature around 15 degrees C at the onset of rigor seems optimal to maximize tenderness without having detrimental effects on water-holding capacity or color.  相似文献   

7.
The objective of the study was to improve the understanding of the relationship between the effect of epinephrine plus exercise and meat tenderness. The calpain, calpastatin, and cathepsin B + L activities and postmortem proteolysis in porcine longissimus muscle were studied. The muscle glycogen stores were depleted in five pigs by s.c. injection of epinephrine (.3 mg/kg) at 15 h antemortem and exercise on a treadmill (5 min, 3.8 km/h) immediately before slaughter. Antemortem injection of epinephrine and treadmill exercise resulted in higher ultimate pH (6.32 vs 5.66 in control) and decreased (P < .05) thaw loss, cooking loss, and shear force values. The muscle energy depletion treatment increased (P < .05) the muscle mu-calpain activity measured 42 min postmortem, and at 24 h mu-calpain activity was still approximately 50% greater in the high ultimate pH group. Also, as the ratio of mu-calpain to calpastatin increased (P < .01), the overall proteolytic potential of the calpain system were greater. These observations suggest that the muscle energy level may influence the activity of the calpain system in the living animal. The high ultimate pH group showed lower (P < .001) cathepsin B + L activity in the myofibrillar and the soluble fractions after 8 d of storage, suggesting that the increased ultimate pH increased the stability of the lysosomal membrane and thereby reduced the release of cathepsins from the lysosomes during storage. The SDS-PAGE showed increased (P < .001) degradation of a 39-kDa band in the epinephrine and exercise-treated samples. Degradation products at 30, 31, and 32 kDa were labeled by troponin-T antibody in western blot. An appearing 24-kDa band was identified as a troponin-I degradation product in western blot. The proteolytic degradation pattern of myofibrillar proteins during storage differed in control and treated samples, supporting the hypothesis that calpain-mediated proteolysis was affected after treatment, resulting in meat with high ultimate pH.  相似文献   

8.
The present study was designed to investigate proteomic differences in duck breast muscle during the early postmortem storage period. The meat quality was evaluated at 0 hr and 24 hr postmortem at 4°C in Pekin ducks, black Muscovy ducks and Mule ducks. Differentially expressed proteins were detected by two‐dimensional gel electrophoresis (2‐DE) and matrix‐assisted laser desorption ionization‐time‐of‐flight mass spectrometry (MALDI‐TOF/TOF MS) at 0 hr and 24 hr postmortem in the three duck breeds. The results showed that 53 proteins spots were differentially expressed at 0 hr and 24 hr postmortem at 4°C in Pekin ducks, 75 spots in black Muscovy ducks, and 72 spots in Mule ducks. A total of 30 (10 spots for each breed) were selected for identification by mass spectrometry. Seven proteins were identified in Pekin ducks, eight in black Muscovy ducks and seven in Mule ducks. Moreover, the above results obtained by 2‐DE and MALDI‐TOF/TOF MS were confirmed by western blotting. To our knowledge, this study is the first to provide insights into the protein profiles of ducks during postmortem storage and provides a better understanding of the biochemical processes that contribute to duck meat quality.  相似文献   

9.
Micro-calpain is essential for postmortem proteolysis of muscle proteins   总被引：1，自引：0，他引：1  
The objective of this investigation was to test the hypothesis that -calpain is largely responsible for postmortem proteolysis of muscle proteins. To accomplish this objective, we compared proteolysis of known muscle proteins in muscles of wild type and micro-calpain knockout mice during postmortem storage. Knockout mice (n = 6) were killed along with control mice (n = 6). Hind limbs were removed and stored at 4 degrees C. Muscles were dissected at 0, 1, and 3d postmortem and subsequently analyzed for degradation of nebulin, dystrophin, metavinculin, vinculin, desmin, and troponin T. In a separate experiment, hind limb muscles from knockout (n = 4) and control mice (n = 4) were analyzed at 0, 1, and 3 d postmortem using casein zymography to confirm that mu-calpain activity was knocked out in muscle and to determine whether or not m-calpain is activated in murine postmortem muscle. Cumulatively, the results of the first experiment indicated that postmortem proteolysis was largely inhibited in micro-calpain knockout mice. The results of the second experiment established the absence of micro-calpain in the muscle tissue of knockout mice and confirmed the results of an earlier study that m-calpain is active in postmortem murine muscle. The results of the current study show that even in a species in which m-calpain is activated to some extent postmortem, micro-calpain is largely responsible for postmortem proteolysis. This observation excludes a major role for any of the other members of the calpain family or any other proteolytic system in postmortem proteolysis of muscle proteins. Therefore, understanding the regulation of micro-calpain in postmortem muscle should be the focus of further research on postmortem proteolysis and tenderization of meat.  相似文献   

10.
The objective of this study was to create various pH/temp decline rates in hot‐boned bull beef M. longissimus lumborum (LL) through a combination of electrical stimulation (ES) and pre‐rigor holding temperature. The relationship between the pre‐rigor interventions, the activities of µ‐calpain and small heat shock proteins (sHSP), and the impacts on meat product quality were determined. Paired LL loins from 13 bulls were hot‐boned within 40 min of slaughter, immediately ES and subjected to various holding temperatures (5, 15, 25, and 35°C) for 3 hr. The rate of muscle pH decline, sarcomere length, shear force, and proteolysis of muscle proteins were measured. ES‐25°C had a longer sarcomere length compared to non‐electrical stimulation samples. ES‐25°C and ES‐35°C samples had lower shear force values, higher µ‐calpain activity and higher desmin, troponin‐T, and sHSP degradation. The above findings suggest that pH/temp decline rates created in hot‐boned muscle impacted muscle protein proteolysis by increasing the activity of proteases and degradation of sHSP.  相似文献   

11.
A negative correlation exists between calpastatin activity and meat tenderness. Therefore, it is important to determine the mechanism of calpastatin inactivation in postmortem skeletal muscle. Western immunoblot analysis was performed to determine the protease(s) responsible for degradation of muscle calpastatin during postmortem storage. To accomplish this, purified calpastatin was digested with different proteases in vitro, and their pattern of calpastatin degradation was compared with that of calpastatin degradation in postmortem muscle. Polyclonal antibodies raised in mice against recombinant bovine skeletal muscle calpastatin were used to monitor calpastatin degradation. Lamb longissimus was stored at 4 degrees C and sampled at 0, 6, 12, 24, 72, 168, and 336 h postmortem. Postmortem storage produced a discrete pattern of calpastatin degradation products that included immunoreactive bands at approximately 100, 80, 65, 54, 32, and 29 kDa. Undegraded calpastatin (130 kDa) was barely detectable after 72 h of postmortem storage at 4 degrees C, and no immunoreactive calpastatin was observed by 336 h postmortem. For in vitro proteolysis, lamb longissimus calpastatin (0 h postmortem) was purified using Affi-Gel Blue chromatography. Calpastatin was digested with m-calpain, mu-calpain, cathepsin B, proteasome, trypsin, or chymotrypsin. Each of these enzymes degraded calpastatin. Immunoreactive fragments resulting from digestion of calpastatin with m- and mu-calpain were similar to each other and closely resembled those observed during postmortem aging of lamb longissimus at 4 degrees C. Digestion of calpastatin with mu-calpain reduced calpastatin activity. Degradation of calpastatin by other proteases resulted in unique patterns of immunoreactive fragments, distinct from that observed in longissimus. Thus, m- and(or) mu-calpain seem to be responsible for calpastatin degradation during postmortem storage of meat.  相似文献   

12.
The aim of the study was to evaluate the impact of 2 isoenergetic growing diets with different CP (17 vs. 23%) on the performance and breast meat quality of 2 lines of chicken divergently selected for abdominal fatness [i.e., fat and lean (LL) lines]. Growth performance, breast and abdominal fat yields, breast meat quality parameters (pH, color, drip loss), and muscle glycogen storage at death were measured. Increased dietary CP resulted in increased BW, increased breast meat yield, and reduced abdominal fatness at slaughter regardless of genotype (P < 0.001). By contrast, dietary CP affected glycogen storage and the related meat quality parameters only in the LL chickens. Giving LL chickens the low-CP diet led to reduced concentration of muscle glycogen (P < 0.01), and as a result, breast meat with a higher (P < 0.001) ultimate pH, decreased (P < 0.001) lightness, and reduced (P < 0.001) drip loss during storage. The decreased muscle glycogen content observed in LL receiving the low-CP diet compared with the high-CP diet occurred concomitantly with greater phosphorylation amount for the α-catalytic subunit of adenosine monophosphate-activated protein kinase and glycogen synthase. This was consistent with the reduced muscle glycogen content observed in LL fed the low-CP diet because adenosine monophosphate-activated protein kinase inhibits glycogen synthesis through its action on glycogen synthase. Our results demonstrated that nutrition is an effective means of modulating breast meat properties in the chicken. The results also highlighted the need to take into account interaction with the genetic background of the animal to select nutritional strategies to improve meat quality traits in poultry.  相似文献   

13.
云南武定鸡肉品质分析   总被引：1，自引：0，他引：1  
本试验对230日龄武定鸡不同性别和部位的肉质物理特性指标进行了测定分析。结果显示:①性别对230日龄武定鸡的肉质物理特性影响不大,仅在嫩度上母鸡优于公鸡,且差异显著(P<0.05);②部位对230日龄武定鸡肉质的物理特性有很明显的影响(P<0.05),胸肌的嫩度、贮藏损失、L值、b值均显著高于腿肌,而a值、pH值显著低于腿肌,只有系水率在胸部和腿部间没有显著差异(P>0.05);③阉割可以改善武定鸡肉质。  相似文献   

14.
钙蛋白酶系统在动物屠宰后肌肉蛋白质水解和肌肉嫩化过程中发挥重要的作用;脂肪酸结合蛋白参与脂肪酸的转运代谢,影响肌肉的嫩度、风味和多汁性,与背膘厚、大理石花纹、嫩度和系水力等肉用性状有较高关联度;生肌调节因子在肌肉分化过程中可控制启动成肌细胞的融合和肌纤维的形成;肌肉生成抑制素是控制肌肉生长的负调控因子,影响畜禽瘦肉率、改善肉质性状的重要营养基因。作者综述了钙蛋白酶系统家族、脂肪酸结合蛋白基因、生肌调节因子和肌肉生长抑制素等影响肉牛肉品质性状的基因,以期在肉牛育种选择中找到使产肉量和肉质得到同步提高的途径,进一步通过标记辅助选择来改善肉牛的肉质性状。  相似文献   

15.
Postmortem changes in osmotic pressure; ionic strength; pH; temperature; mu- and m-calpain; calpastatin; desmin degradation; and myofibril fragmentation index (MFI) were determined in ovine longissimus muscle. Our objectives were to characterize changes in these variables and to identify postmortem time points at which significant proteolysis and tenderization (as measured by change in MFI) could be detected. Seven crossbred (Dorset x Romanov) lambs were slaughtered, and samples of the longissimus muscle were removed at 0, 3, 6, 9, 12, 24, 72, and 360 h postmortem. Osmotic pressure increased (P < 0.05) from 379 to 528 mOsm during the postmortem storage period, with two-thirds of the increase occurring within the first 24 h. By measuring conductivity, we showed that ionic strength increased (P < 0.05) from 8.13 to 9.78 mS/cm during the storage period, which is equivalent to 79 and 97 mM NaCl solutions, respectively. In accordance with pH and temperature, conductivity reached ultimate levels at 24 h postmortem. Within 9 h postmortem, mu-calpain activity had decreased (P < 0.05) from at-death values and continued to decrease until 72 h, at which time it was undetectable. It was still possible to detect the 76-kDa isoforms (a product of the autolysis of the 80-kDa subunit of mu-calpain) immunologically, which implies that the loss of activity was not caused by extensive autolysis. In contrast, m-calpain activity remained constant throughout the aging period, whereas calpastatin activity was stable until 24 h postmortem, after which it gradually decreased. Autolysis products of mu-calpain were detected at 3 h postmortem, indicating that mu-calpain was activated some time between 0 and 3 h postmortem. Moreover, the effect of mu-calpain activity on myofibrillar substrates was first observed at 9 h postmortem, when a 23% loss of native desmin was detected. This degradation translated into an increase in MFI at 12 h. Collectively, these results imply that mu-calpain is active in postmortem muscle in the presence of calpastatin, and that effects of mu-calpain activity as determined by increased MFI are detectable during the first 12 h postmortem.  相似文献   

16.
The water‐holding capacity (WHC), and toughness (shear force) of chicken gizzard were evaluated during postmortem storage for 4.5, 7, 12, 24, 48, 72 and 96 h at 4°C. Degradation of the cytoskeletal proteins desmin, talin and vinculin were monitored by sodium dodecyl sulfate – polyacrylamide gel electrophoresis and Western blotting during the same designated storage period. The WHC of the gizzards decreased significantly from 12 h to 72 h of storage, but by 96 h the WHC was restored to the level measured after storage for 12 h. The shear force value of the gizzards increased rapidly until 12 h and then decreased until 24 h, with a further slight decrease by 48 h. Degradation products of desmin, talin and vinculin appeared at 96 h, 12 h and 48 h postmortem, respectively. The intensity of immunolabeling for desmin, talin and vinculin after storage for 96 h decreased to 51%, 25% and 52% of the initial value. The appearance of desmin degradation products was accompanied by an increase in WHC. This suggests that the postmortem degradation of desmin is involved in the increase of WHC in chicken gizzard during storage at 4°C, and talin and vinculin may be involved.  相似文献   

17.
An in situ system involving incubation of 60- to 80-g pieces of muscle at 4 degrees C under different conditions was used to determine the effects of time of postmortem storage, of pH, and of temperature on activities of mu- and m-calpain activity in bovine skeletal muscle. Casein zymograms were used to allow measurement of calpain activity with a minimum of sample preparation and to ensure that the calpains were not exposed to ionic strengths of 100 or greater before assay of their activities. In 4 of the 5 muscles (longissimus dorsi, lumbar; longissimus dorsi, thoracic; psoas major; semimembranosus; and triceps brachii) studied, mu-calpain activity decreased nearly to zero within 48 h postmortem. Activity of m-calpain also decreased in the in situ system used but at a much slower rate. Activities of both mu- and m-calpain decreased more slowly in the triceps brachii muscle than in the other 4 muscles during postmortem storage. Although previous studies have indicated that mu-calpain but not m-calpain is proteolytically active at pH 5.8, these studies have used calpains obtained from muscle at death. Both mu- and m-calpain are proteolytically inactive if their activities are measured at pH 5.8 and after incubating the muscle pieces for 24 h at pH 5.8. Western analysis suggested that neither the large 80-kDa subunit nor the small 28-kDa subunit of m-calpain was autolyzed during postmortem storage of the muscle pieces. As has been reported previously, the 80-kDa subunit of mu-calpain was autolyzed to 78- and then to a 76-kDa polypeptide after 7 d postmortem, but the 28-kDa small subunit was not autolyzed; hence, the autolyzed mu-calpain molecule in postmortem muscle is a 76-/28-kDa molecule and not a 76-/18-kDa molecule as previously assumed. Because both subunits were present in the postmortem calpains, loss of mu-calpain activity during postmortem storage is not due to dissociation of the 2 subunits and inactivation. Although previous studies have shown that the 76-/18-kDa mu-calpain molecule is completely active proteolytically, it is possible that the 76-/28-kDa mu-calpain molecule in postmortem muscle is proteolytically inactive and that this accounts for the loss of mu-calpain activity during postmortem storage. Because neither mu- nor m-calpain is proteolytically active at pH 5.8 after being incubated at pH 5.8 for 24 h, other proteolytic systems such as the caspases may contribute to postmortem proteolysis in addition to the calpains.  相似文献   

18.
为深入了解家禽肉品质性状形成的分子机制,本实验测定金茅黑鸡胸肌的肉品质,利用RNA-seq技术进行转录组测序,分析转录组基因表达量与肉品质性状间的关联性。结果显示:与金茅黑鸡14周龄肉色显著相关的基因5个,pH57个,剪切力33个,系水力17个;PLEKHS1、MUC等基因为影响肉色的候选基因,LHX9、SPDEF、GRXCR1等基因为系水力的候选基因,NPY、POMC、FGF20、MGAT4C和GUK1基因为影响肌肉pH的候选基因,EDAR基因和HS6ST3基因为肌肉剪切力的主要候选基因;功能分析发现这些基因在调节肌肉纤维、肌间脂肪沉积、脂类代谢、糖代谢过程和磷酸二酯酶水解等方面发挥重要作用,进而影响胸肌肌肉品质的形成。  相似文献   

19.
We evaluated effects of dietary supplementation with astaxanthin (Ax)‐rich yeast, Phaffia rhodozyma (Xanthophyllomyces dendrorhous), on broiler chicken meat quality. Fourteen‐day‐old female Ross broilers were divided into three groups: control group, Ax‐free diet; Ax 10 group, 10 mg/kg Ax diet; and Ax 20 group, 20 mg/kg Ax diet for 28 days. At 42 days old, chickens were slaughtered, and then growth performance, meat quality and sensory attributes were analyzed. Compared with the control, a* values increased significantly after slaughter and 48 h postmortem for Ax 20 samples (P < 0.05) and for b* values in Ax 20 and Ax 10 groups (P < 0.05). Cooking loss decreased in the Ax 20 group (P < 0.05). After 120 h aging, contents of several free amino acids and total free amino acid content of Ax 20 group were significantly higher than the control (P < 0.05). In sensory evaluation, meat texture attributes improved significantly in the Ax 20 group (P < 0.01). No significant changes occurred in flavor attribute scores of meat soup from the Ax 20 group compared with the control even though most assessors preferred meat soup from the Ax 20 group. Overall, Ax‐rich yeast in the diet improves broiler chicken meat quality.  相似文献   

20.
Casein zymography was used to determine the effect of postmortem storage on the proteolytic activity of mu-calpain and m-calpain in lamb longissimus. Casein zymography assays were conducted on crude muscle extracts (only one centrifugation). Six market weight crossbred lambs were slaughtered and a portion of the longissimus lumborum was removed at death (within 15 min of exsanguination) and after 3, 6, 9, 12, 24, 72, and 360 h postmortem. Muscle samples were snap-frozen in liquid nitrogen and stored at -70 degrees C. Soluble muscle proteins were extracted from muscle samples and analyzed by in-gel casein assay to measure calpain proteolytic activity. There was a gradual decline in mu-calpain activity (P < 0.05) such that after 24 and 72 h postmortem, mu-calpain had lost 42 and 95% of its activity, respectively. After 360 h postmortem, no mu-calpain activity could be detected (under the conditions used in this study). Autolysis of mu-calpain could be detected as early as 3 h postmortem. It was demonstrated that the detectable level of mu-calpain activity is a function of the amount of muscle protein electrophoresed. Hence, the activity data reported are in relative terms, rather than absolute values. Furthermore, it was demonstrated that the activity data also are a function of the assay methods used. Different methods have different lower detection limits. Of the three assays examined, 14C-labeled casein was the most sensitive, then the in-gel casein assay, and the least-sensitive method was the standard casein assay. Unlike mu-calpain, postmortem storage had no effect on m-calpain (P > 0.05). When the calcium concentration of a muscle extract was increased to the level that induces m-calpain autolysis, m-calpain was autolyzed and its autolysis was readily detected by the in-gel casein assay. Collectively, these results demonstrate that calcium concentration in postmortem muscle is only high enough to activate mu-calpain. These results support the widely believed conclusion that mu-calpain-mediated proteolysis of key myofibrillar and cytoskeletal proteins is responsible for postmortem tenderization. Hence, understanding the regulation of mu-calpain in postmortem muscle should be the focus of future studies.  相似文献   

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