Proteolytic degradation of isolated myofibrils and myofibrillar proteins by m-calpain from the skeletal muscle of the amphibianRana ridibunda

Sargianos, N.; Gaitanaki, Catherine; Dimitriadis, B.K.; Beis, Isidoros

doi:10.1002/(sici)1097-010x(19960901)276:1<30::aid-jez4>3.0.co;2-6

Cited by 8 publications

(2 citation statements)

References 53 publications

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“…The activity of sea bass m‐calpain towards the myofibrillar protein fraction from the same tissue is summarised in Table 1 and compared with results obtained for other animals 24. 27, 34, 35 As can be seen, m‐calpain from mammalian sources does not have the same effect as sea bass m‐calpain on some myofibrillar proteins.…”

Section: Resultsmentioning

confidence: 99%

In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus Labrax L) by an endogenous m‐calpain

et al. 2002

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The effects of m-calpain isolated from the skeletal muscle of sea bass on sarcoplasmic and myofibrillar proteins isolated from the same tissue were examined in vitro. Incubation of sarcoplasmic proteins with m-calpain resulted in only a slight decrease (0.7 kDa) in the molecular weight (MW) of a 26.5 kDa protein. Degradation of myofibrils, monitored by quantification of TCA-soluble peptides generated, resulted in the maximum amount of peptides being generated after 1 h of incubation at 25°C. Noticeable modifications in the SDS-PAGE profile of digested myofibrils were observed, including partial denaturation of myosin heavy chain and the release of tropomyosin, $69 and $27 kDa doublet bands and a few polypeptides of MW lower than 20 kDa in the soluble fraction. Examination of the degradation patterns of myofibrillar proteins using Western blotting showed that a-actinin was partially degraded, with release of native a-actinin and its fragments from myofibrils, whereas desmin was highly degraded after 2 h of digestion.

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Section: Resultsmentioning

confidence: 99%

In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus Labrax L) by an endogenous m‐calpain

et al. 2002

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“…The indigenous proteinases that are involved in turnover and growth of muscle proteins contribute to the postmortem meat tenderization (Goll et al, 1992;Koohmaraie, 1992). Meat tenderness is found to be highly correlated with the proteolytic breakdown of myofibrillar proteins, disappearance of Z-lines, and disassembly of sarcomeric protein (Huang et al, 1998;Morton et al, 1999;Sargianos et al, 1996). According to Crouse and Koohmaraie (1990), postmortem beef became tender when calpastatin failed to regulate calpain hydrolytic activity.…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of Calpastatin from Grass Prawn Muscle (Penaeus monodon)

Jiang

et al. 2000

J. Agric. Food Chem.

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Calpastatin, a specific calpain inhibitor was purified to electrophoretical homogeneity from grass prawn (Penaeus monodon) muscle by 100 degrees C heat-treatment, DEAE-Sephacel, and Q-Sepharose chromatographs. No significant change in the inhibitory activity of crude calpastatin was observed even after 20 min incubation at 100 degrees C, pH 7.0. The purified prawn calpastatin had a molecular weight (M(r)) of 80 and 88.7 kDa determined by SDS-PAGE and Sephacryl S-200 HR gel filtration, respectively. According to the active site titration, the purified calpastatin revealed four beef mu-calpain and two beef m-calpain binding domains, respectively. It was stable during 1 h of incubation at 30 degrees C under pH 4.5-10.0 and shown to be a highly specific inhibitor for calpain.

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Effect of lactic or acetic acid on degradation of myofibrillar proteins in post-mortem goose (Anser anser) breast muscle

Hwang¹,

Lin

Chou

2000

J. Sci. Food Agric.

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Proteolytic degradation of isolated myofibrils and myofibrillar proteins by m-calpain from the skeletal muscle of the amphibianRana ridibunda

Cited by 8 publications

References 53 publications

In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus Labrax L) by an endogenous m‐calpain

In vitro proteolysis of myofibrillar and sarcoplasmic proteins of European sea bass (Dicentrarchus Labrax L) by an endogenous m‐calpain

Purification and Characterization of Calpastatin from Grass Prawn Muscle (Penaeus monodon)

Effect of lactic or acetic acid on degradation of myofibrillar proteins in post-mortem goose (Anser anser) breast muscle

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