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Analysis of Methionine Oxidation in Myosin Isoforms in Porcine Skeletal Muscle by LC-MS/MS Analysis
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) w...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Korean Society for Food Science of Animal Resources
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4869553/ https://www.ncbi.nlm.nih.gov/pubmed/27194935 http://dx.doi.org/10.5851/kosfa.2016.36.2.254 |
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author | Jeong, Jin-Yeon Jung, Eun-Young Jeong, Tae-Chul Yang, Han-Sul Kim, Gap-Don |
author_facet | Jeong, Jin-Yeon Jung, Eun-Young Jeong, Tae-Chul Yang, Han-Sul Kim, Gap-Don |
author_sort | Jeong, Jin-Yeon |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4869553 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Korean Society for Food Science of Animal Resources |
record_format | MEDLINE/PubMed |
spelling | pubmed-48695532016-05-18 Analysis of Methionine Oxidation in Myosin Isoforms in Porcine Skeletal Muscle by LC-MS/MS Analysis Jeong, Jin-Yeon Jung, Eun-Young Jeong, Tae-Chul Yang, Han-Sul Kim, Gap-Don Korean J Food Sci Anim Resour Article 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. Korean Society for Food Science of Animal Resources 2016 2016-04-30 /pmc/articles/PMC4869553/ /pubmed/27194935 http://dx.doi.org/10.5851/kosfa.2016.36.2.254 Text en Copyright © 2016, Korean Society for Food Science of Animal Resources http://creativecommons.org/licences/by-nc/3.0 This is an open access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licences/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Article Jeong, Jin-Yeon Jung, Eun-Young Jeong, Tae-Chul Yang, Han-Sul Kim, Gap-Don Analysis of Methionine Oxidation in Myosin Isoforms in Porcine Skeletal Muscle by LC-MS/MS Analysis |
title | Analysis of Methionine Oxidation in Myosin Isoforms in Porcine Skeletal Muscle by LC-MS/MS Analysis |
title_full | Analysis of Methionine Oxidation in Myosin Isoforms in Porcine Skeletal Muscle by LC-MS/MS Analysis |
title_fullStr | Analysis of Methionine Oxidation in Myosin Isoforms in Porcine Skeletal Muscle by LC-MS/MS Analysis |
title_full_unstemmed | Analysis of Methionine Oxidation in Myosin Isoforms in Porcine Skeletal Muscle by LC-MS/MS Analysis |
title_short | Analysis of Methionine Oxidation in Myosin Isoforms in Porcine Skeletal Muscle by LC-MS/MS Analysis |
title_sort | analysis of methionine oxidation in myosin isoforms in porcine skeletal muscle by lc-ms/ms analysis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4869553/ https://www.ncbi.nlm.nih.gov/pubmed/27194935 http://dx.doi.org/10.5851/kosfa.2016.36.2.254 |
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