2001
DOI: 10.1046/j.1444-2906.2001.00345.x
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Effects of urea and trimethylamine-N-oxide on ATPase of requiem shark myofibril and its constituents

Abstract: The effects of trimethylamine‐N‐oxide (TMAO) on the urea‐resistibility of requiem shark myofibrils were investigated, using Ca2+‐ and Mg2+‐ATPase activities as a parameter. Both activities were hardly changed or activated up to 0.6 M urea. In contrast, the two activities both decreased to less than 50% in the presence of TMAO up to 0.5 M. When measured at a 2 : 1 molar ratio of urea and TMAO, Ca2+‐ and Mg2+‐ATPase activities were similar to those in the presence of TMAO alone, indicating that TMAO reduced the … Show more

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Cited by 6 publications
(7 citation statements)
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“…Urea is a well‐known protein denaturant, which might change the structure of most proteins including myofibrillar protein in muscle (Kanoh et al . ). Mathew et al .…”
Section: Resultsmentioning
confidence: 97%
See 1 more Smart Citation
“…Urea is a well‐known protein denaturant, which might change the structure of most proteins including myofibrillar protein in muscle (Kanoh et al . ). Mathew et al .…”
Section: Resultsmentioning
confidence: 97%
“…Moreover, shark mince at day 0 contained urea at high concentration. Urea is a well-known protein denaturant, which might change the structure of most proteins including myofibrillar protein in muscle (Kanoh et al 2001). Mathew et al (2002) reported that the addition of urea at levels of 250-1,000 mM into shark myofibrillar protein lowered its gelling ability.…”
Section: Effect Of Mtgase On Gel Properties Of Mince and Washed Mincementioning
confidence: 99%
“…The other strategy is the evolution of a protein structure that resists urea denaturation. Banded houndshark fast skeletal myofibrils show urea-resistibility for Ca 2+ - and Mg 2+ -ATPase activities, suggesting that myofibril components, especially myosin molecules, have native urea-resistibility 15 , 16 . Banded houndshark myosin has been shown to exhibit native ATPase activity in the presence of 0.3 M urea, which is close to the physiological concentration in muscle tissue, whereas carp myosin loses 70% of its ATPase activity at this urea concentration 16 .…”
Section: Introductionmentioning
confidence: 99%
“…Banded houndshark myosin has been shown to exhibit native ATPase activity in the presence of 0.3 M urea, which is close to the physiological concentration in muscle tissue, whereas carp myosin loses 70% of its ATPase activity at this urea concentration 16 . For banded houndshark myosin, TMAO cannot neutralize the urea effect on myosin ATPase activity but actually inhibits the activity of this enzyme 15 . These findings might indicate that the molecular structure of elasmobranch myosin provides urea-resistibility to myosin molecules.…”
Section: Introductionmentioning
confidence: 99%
“…Trimethylamine‐ N ‐oxide (TMAO) is a common and compatible osmolyte in tissues of marine organisms, and counteracts the effects of protein destabilizing agents such as urea in elasmobranchs 1,2 and of hydrostatic pressure on enzyme function in deep‐sea animals 3,4 . Gadoid fish are commercially important species including walleye pollack, cod, hake, whiting and haddock, which have high levels of TMAO in their muscles.…”
Section: Introductionmentioning
confidence: 99%