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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2016.1
- 수록면
- 254 - 261 (8page)
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초록· 키워드
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The purpose of this study was to analyze oxidized methionines in the myosin isoforms of porcine longissimus thoracis, psoas major, and semimembranosus muscles by liquid chromatography (LC) and mass spectrometry (MS). A total of 836 queries matched to four myosin isoforms (myosin-1, -2, -4, and -7) were analyzed and each myosin isoform was identified by its unique peptides (7.3-13.3). Forty-four peptides were observed from all three muscles. Seventeen peptides were unique to the myosin isoform and the others were common peptides expressed in two or more myosin isoforms. Five were identified as oxidized peptides with one or two methionine sulfoxides with 16 amu of mass modification. Methionines on residues 215 (215), 438 (438), 853 (851), 856 (854), 1071 (1069), and 1106 (1104) of myosin-1 (myosin-4) were oxidized by the addition of oxygen. Myosin-2 had two oxidized methionines on residues 215 and 438. No queries matched to myosin-7 were observed as oxidized peptides. LC-MS/MS allows analysis of the oxidation of specific amino acids on specific residue sites, as well as in specific proteins in the food system.
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참고문헌 (43)
참고문헌 신청
Abreu, E. / 2006 / Myosin heavy chain fibre types and fibre sizes in nulliparous and primiparous ovariectomized Iberian sows: Interaction with two alternative rearing systems during the fattening period / Meat Sci 74:359~372
Armenteros, M. / 2009 / Analysis of protein carbonyls in meat products by using the DNPH method, fluorescence spectroscopy and liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) / Meat Sci 83:104~112
Bernevic, B. / 2011 / Degradation and oxidation postmortem of myofibrillar proteins in porcine skeleton muscle revealed by high resolution mass spectrometric proteome analysis / Int. J. Mass Spectrom 305:217~227
Bradford, M. M. / 1976 / A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72:248~254
Chang, K. C. / 2003 / Relationships of myosin heavy chain fibre types to meat quality traits in traditional and modern pigs / Meat Sci 64:93~103
Armenteros, M. / 2009 / Analysis of protein carbonyls in meat products by using the DNPH method, fluorescence spectroscopy and liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS) / Meat Sci 83:104~112
Bernevic, B. / 2011 / Degradation and oxidation postmortem of myofibrillar proteins in porcine skeleton muscle revealed by high resolution mass spectrometric proteome analysis / Int. J. Mass Spectrom 305:217~227
Bradford, M. M. / 1976 / A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72:248~254
Chang, K. C. / 2003 / Relationships of myosin heavy chain fibre types to meat quality traits in traditional and modern pigs / Meat Sci 64:93~103
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