Structural differences between myofibrillar protein, paratropomyosin, and tropomyosin as revealed by high‐performance liquid chromatography

Nishio, Yuriko; Ushimura, Yuichi; Ueda, Shuji; Maeda, Naoyuki; Hattori, Akihito; Yamanoue, Minoru

doi:10.1111/asj.13022

Cited by 2 publications

(4 citation statements)

References 26 publications

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“…In our study, all separated peak bands were moved to 34 kDa in SDS‐PAGE (Figures and ). This result was compatible with Roy, Potter, and Sarkar () and Nishio et al ().…”

Section: Resultssupporting

confidence: 92%

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Evaluation of antioxidant level and protein oxidation of rainbow trout (Oncorhynchus mykiss) fillets during rigor and post‐rigor

Isık

Atamanalp

Alak

2019

Journal of Food Safety

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In this study, the relationship between stunning techniques and protein oxidation which are accepted as the main cause of food spoilage was investigated. For this purpose, the antioxidant status, in vivo myofibrillary protein (MP) oxidation and sensitivity, and postmortem oxidation (inducted with hydroxyl radical system) of rainbow trout (Oncorhynchus mykiss) fillets killed by hitting to head (T1), neck crushing (T2), and convulsion (T3) methods, were investigated. Statistically significant differences (p < .05) were found among all parameters examined and it was observed that the most stressing technique was the convulsion method. It was determined that in protein profiles myosin were influenced too much from stunning technique and in actin observed oxidation-induced reductions. Reductions in S-S and S-H were also found to be increased in carbonyl concentrations, but the most effective values in both processes were determined by the convulsive technique. Our results show that shortterm stunning techniques (hitting to head, neck crushing) give better meat quality results in terms of O. mykiss welfare and low MP oxidation rates. In general, we can say that T3 group fillets are more sensitive to oxidative damage, while T1 and T2 groups give better results in maintaining meat quality with low MP oxidation rates.

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“…In our study, all separated peak bands were moved to 34 kDa in SDS‐PAGE (Figures and ). This result was compatible with Roy, Potter, and Sarkar () and Nishio et al ().…”

Section: Resultssupporting

confidence: 92%

“…TM is a regulatory protein of myofibrils and has been reported as the standard structure of a coiled coil with two subunits (Nishio et al, ). In our study, all separated peak bands were moved to 34 kDa in SDS‐PAGE (Figures and ).…”

Section: Resultsmentioning

confidence: 99%

Evaluation of antioxidant level and protein oxidation of rainbow trout (Oncorhynchus mykiss) fillets during rigor and post‐rigor

Isık

Atamanalp

Alak

2019

Journal of Food Safety

View full text Add to dashboard Cite

show abstract

“…In our study, all separated peak bands were moved to 34 kDa in SDS‐PAGE (Figures and ). This result was compatible with Roy, Potter, and Sarkar (), Nishio et al () and Ölmez and Alak ().…”

Section: Resultssupporting

confidence: 91%

“…In addition, muscle structure may also cause this (Torres de Souza Rodrigues et al, ). Tropomyosin (TM) is a regulatory protein of myofibrils and has been reported as the standard structure of a coil with two subunits (Nishio et al, ). In our study, all separated peak bands were moved to 34 kDa in SDS‐PAGE (Figures and ).…”

Section: Resultsmentioning

confidence: 99%

Determining protein denaturation of sardine (Sardina pilchardus) marinates before and after the maturation

Dericioglu

Alak

Atamanalp

2019

J Food Process Preserv

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In this study, sardine fish (Sardina pilchardus) was subjected to marination at different degrees of acidity (2.5%–5%). On the basis of the duration of maturation (22 days) and postmaturation period (three months after maturation), protein denaturation and quality changes of marinades were determined. Quality parameters, such as pH, acidity, salinity, and lipid oxidation, were examined for both periods. As a result of the study carried out for 22 days at different acidity levels, the change in the amount of TVB‐N was found to be insignificant (p > 0.05), but the differences in pH, TBARS, acidity, and salinity levels were found to be significant (p < 0.05). In the postmaturation period, the change in the TBARS amount was insignificant (p > 0.05), and the other parameters were found to be significant (p < 0.05). SDS‐PAGE analysis showed that fish muscle and brine proteins showed different profiles and a decrease in densities of MHC, actin, and TM bands during the maturation period was observed. Practical applications Protein denaturation is important in fisheries products, so multiple verification tests should be performed to monitor this process. It was suggested that DSC and SDS‐PAGE techniques are easier and quicker analyses for determining protein denaturation in seafood products compared with traditional techniques.

show abstract

Structural differences between myofibrillar protein, paratropomyosin, and tropomyosin as revealed by high‐performance liquid chromatography

Cited by 2 publications

References 26 publications

Evaluation of antioxidant level and protein oxidation of rainbow trout (Oncorhynchus mykiss) fillets during rigor and post‐rigor

Evaluation of antioxidant level and protein oxidation of rainbow trout (Oncorhynchus mykiss) fillets during rigor and post‐rigor

Determining protein denaturation of sardine (Sardina pilchardus) marinates before and after the maturation

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