Early Structural Changes in Myosin Rod upon Heating of Carp Myofibrils

Konno, Kunihiko; Yamamoto, Takeshi; Takahashi, Masayuki; Kato, Sanae

doi:10.1021/jf990479i

Cited by 20 publications

(34 citation statements)

References 19 publications

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“…3 It is also accepted that myosin denaturation in fish meat affects the quality of its final products. 7 By using this method, we found that rod denaturation preceded S-1 denaturation in carp myofibrils. 4 As used in the present case, Ca 2+ -ATPase inactivation has been used widely as an index for myosin denaturation.…”

Section: Introductionmentioning

confidence: 90%

Denaturation mode of carp myofibrils when affected by temperature and salt concentration

Yamamoto¹,

Takahashi²,

Kato³

et al. 2002

Fisheries Sci

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Heating temperatures of 30–40°C and KCl concentrations of 0.1–0.5 M altered the denaturation mode of carp myofibrils. In 0.1 M KCl medium, heating temperature affected the denaturation of rod more significantly than of subfragment‐1 (S‐1), and a slow decrease in solubility at 30°C was accompanied by a slow denaturation of rod. KCl concentration at heating altered the denaturation mode differently at 30°C and 40°C. Increased KCl concentrations for heating reduced the rod denaturation rate at 40°C, but it was increased at 30°C. At concentrations above 0.3*Τ*M KCl, the denaturation rate for rod became identical to that for S‐1 at both temperatures. Upon heating of chymotryptic digest of myofibrils, S‐1 denaturation was similarly detected as in intact myofibrils, whereas practically no rod denaturation was detected. Thus, it was concluded that myosin structure connecting S‐1 and rod has an important role in the denaturation process.

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Section: Introductionmentioning

confidence: 90%

Denaturation mode of carp myofibrils when affected by temperature and salt concentration

Yamamoto¹,

Takahashi²,

Kato³

et al. 2002

Fisheries Sci

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“…Quick decrease of rod production was accompanied by the production of LMM-like or subgfragment-2-like fragments migrating above actin band as proved with fish myofibrils [8]. The pattern found in Ca-medium was similar to that of carp myofibrils and slow rod denaturation in ED-medium was rather similar to that of pollock myofibrils [9].…”

Section: Discussionmentioning

confidence: 60%

“…We proposed that chymotryptic digestion of myofibrils detects myosin denaturation at rod portion as well as head region by their decreased production [8].…”

Section: Introductionmentioning

confidence: 99%

Effect of calcium ion on the thermal denaturation of subfragment-1 and rod regions of squid myosin upon the heating of myofibrils

Abe

Kinoshita²,

Konno

2011

Fish Sci

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Ca 2+ -ATPase inactivation in Ca-medium, which was well explained by the fast rod denaturation. In contrast, rod denaturation was slower than S-1 in EDTA-medium.Decrease in monomeric myosin content was explained by faster S-1 denaturation.Comparing the S-1 and rod denaturation rates at the fixed temperature, it was concluded that S-1 denaturation was suppressed by Ca 2+ whereas rod portion was not. Unfolding experiment with isolated myosin rod confirmed no stabilizing effect of Ca 2+ on rod. It was concluded that significant stabilization of S-1 portion by Ca 2+ generated apparently different myosin denaturation pattern in two media.

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“…Increased digestibility of myofibrils upon heating was the consequence of the exposure of new cleavage sites on myosin molecule to cystein-and serine-types as observed in chymotryptic digestion of heated myofibrils [17]. However, the same structural change of myosin did not expose new cleavage sites for metallo-type, and rather suppressed.…”

Section: Discussionmentioning

confidence: 87%

Three types of proteinases in Japanese common squid Todarodes pacificus hepatopancreas as studied by using carp myofibrils as substrate

et al. 2010

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Three types of proteinases, namely cystein-, metallo-, and serine-proteinases were found in squid hepatopancreas by studying the inhibition spectra using carp myofibril as substrates. Cystein-, metallo-, and serine-type showed the highest activities at 50 ºC, 35 ºC, and 40 ºC, respectively. The optimal pHs were pH 5, pH 7, and pH 9 for cystein-, metallo-, and serine-type, respectively. When assayed at 20 ºC and pH7.5, metallo-type showed the highest activity. Metallo-type was characterized by a high selectivity in the digestion of myosin. Among the three enzymes, cystein-type was found to be the most stable against thermal and acid treatments. Heat treated myofibrils were more susceptible to cystein-and serine-types, but less susceptible to metallo-type. Acid treatment of myofibrils also enhanced the digestibility by cystein-type. The results indicated that cystein-type seemed to be the most suitable enzyme to produce peptides from denatured myofibrils by their random digestion.

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Early Structural Changes in Myosin Rod upon Heating of Carp Myofibrils

Cited by 20 publications

References 19 publications

Denaturation mode of carp myofibrils when affected by temperature and salt concentration

Denaturation mode of carp myofibrils when affected by temperature and salt concentration

Effect of calcium ion on the thermal denaturation of subfragment-1 and rod regions of squid myosin upon the heating of myofibrils

Three types of proteinases in Japanese common squid Todarodes pacificus hepatopancreas as studied by using carp myofibrils as substrate

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