Assessment of RNAlater<sup>®</sup> as a Potential Method to Preserve Bovine Muscle Proteins Compared with Dry Ice in a Proteomic Study
RNAlater<sup>®</sup> is regarded as a potential preservation method for proteins, while its effect on bovine muscle proteins has rarely been evaluated. Bovine muscle protein samples (<i>n</i> = 12) collected from three tender (Warner⁻Bratzler shear force: 3...
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| Format: | Article |
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MDPI AG
2019-02-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/8/2/60 |
| _version_ | 1818518338417983488 |
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| author | Yao Zhu Anne Maria Mullen Dilip K. Rai Alan L. Kelly David Sheehan Jamie Cafferky Ruth M. Hamill |
| author_facet | Yao Zhu Anne Maria Mullen Dilip K. Rai Alan L. Kelly David Sheehan Jamie Cafferky Ruth M. Hamill |
| author_sort | Yao Zhu |
| collection | DOAJ |
| description | RNAlater<sup>®</sup> is regarded as a potential preservation method for proteins, while its effect on bovine muscle proteins has rarely been evaluated. Bovine muscle protein samples (<i>n</i> = 12) collected from three tender (Warner⁻Bratzler shear force: 30.02⁻31.74 N) and three tough (Warner⁻Bratzler shear force: 54.12⁻66.25 N) Longissimus thoracis et lumborum (LTL) samples, preserved using two different sampling preservation methods (RNAlater<sup>®</sup> and dry ice), at two <i>post mortem</i> time points (day 0 and day 14), were characterized using one-dimensional electrophoresis. Fourteen bands with molecular weights ranging from 15 to 250 kDa were verified, both in the dry ice and RNAlater<sup>®</sup> storage groups, at each time point, using image analysis. A shift from high to low molecular weight fragments, between day 0 and day 14, indicated proteolysis of the muscle proteins during post mortem storage. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses and database searching resulted in the identification of 10 proteins in four bands. Protein profiles of muscle preserved in RNAlater<sup>®</sup> were similar to those of muscle frozen on dry ice storage, both at day 0 and day 14. The results demonstrate that RNAlater<sup>®</sup> could be a simple and efficient way to preserve bovine muscle proteins for bovine muscle proteomic studies. |
| first_indexed | 2024-12-11T01:08:56Z |
| format | Article |
| id | doaj.art-9f52ed775cd345459fff5069d8ffb1d7 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-12-11T01:08:56Z |
| publishDate | 2019-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-9f52ed775cd345459fff5069d8ffb1d72022-12-22T01:26:06ZengMDPI AGFoods2304-81582019-02-01826010.3390/foods8020060foods8020060Assessment of RNAlater<sup>®</sup> as a Potential Method to Preserve Bovine Muscle Proteins Compared with Dry Ice in a Proteomic StudyYao Zhu0Anne Maria Mullen1Dilip K. Rai2Alan L. Kelly3David Sheehan4Jamie Cafferky5Ruth M. Hamill6Teagasc Food Research Centre, Ashtown, Dublin D15KN3K, IrelandTeagasc Food Research Centre, Ashtown, Dublin D15KN3K, IrelandTeagasc Food Research Centre, Ashtown, Dublin D15KN3K, IrelandSchool of Food and Nutritional Sciences, University College Cork, Cork T12 K8AF, IrelandDepartment of Chemistry, Khalifa University, Abu Dhabi PO Box 127788, UAETeagasc Food Research Centre, Ashtown, Dublin D15KN3K, IrelandTeagasc Food Research Centre, Ashtown, Dublin D15KN3K, IrelandRNAlater<sup>®</sup> is regarded as a potential preservation method for proteins, while its effect on bovine muscle proteins has rarely been evaluated. Bovine muscle protein samples (<i>n</i> = 12) collected from three tender (Warner⁻Bratzler shear force: 30.02⁻31.74 N) and three tough (Warner⁻Bratzler shear force: 54.12⁻66.25 N) Longissimus thoracis et lumborum (LTL) samples, preserved using two different sampling preservation methods (RNAlater<sup>®</sup> and dry ice), at two <i>post mortem</i> time points (day 0 and day 14), were characterized using one-dimensional electrophoresis. Fourteen bands with molecular weights ranging from 15 to 250 kDa were verified, both in the dry ice and RNAlater<sup>®</sup> storage groups, at each time point, using image analysis. A shift from high to low molecular weight fragments, between day 0 and day 14, indicated proteolysis of the muscle proteins during post mortem storage. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses and database searching resulted in the identification of 10 proteins in four bands. Protein profiles of muscle preserved in RNAlater<sup>®</sup> were similar to those of muscle frozen on dry ice storage, both at day 0 and day 14. The results demonstrate that RNAlater<sup>®</sup> could be a simple and efficient way to preserve bovine muscle proteins for bovine muscle proteomic studies.https://www.mdpi.com/2304-8158/8/2/60muscle proteinsone-dimensional electrophoresisbovine proteomicsLC-MS/MSsample preparation |
| spellingShingle | Yao Zhu Anne Maria Mullen Dilip K. Rai Alan L. Kelly David Sheehan Jamie Cafferky Ruth M. Hamill Assessment of RNAlater<sup>®</sup> as a Potential Method to Preserve Bovine Muscle Proteins Compared with Dry Ice in a Proteomic Study Foods muscle proteins one-dimensional electrophoresis bovine proteomics LC-MS/MS sample preparation |
| title | Assessment of RNAlater<sup>®</sup> as a Potential Method to Preserve Bovine Muscle Proteins Compared with Dry Ice in a Proteomic Study |
| title_full | Assessment of RNAlater<sup>®</sup> as a Potential Method to Preserve Bovine Muscle Proteins Compared with Dry Ice in a Proteomic Study |
| title_fullStr | Assessment of RNAlater<sup>®</sup> as a Potential Method to Preserve Bovine Muscle Proteins Compared with Dry Ice in a Proteomic Study |
| title_full_unstemmed | Assessment of RNAlater<sup>®</sup> as a Potential Method to Preserve Bovine Muscle Proteins Compared with Dry Ice in a Proteomic Study |
| title_short | Assessment of RNAlater<sup>®</sup> as a Potential Method to Preserve Bovine Muscle Proteins Compared with Dry Ice in a Proteomic Study |
| title_sort | assessment of rnalater sup r sup as a potential method to preserve bovine muscle proteins compared with dry ice in a proteomic study |
| topic | muscle proteins one-dimensional electrophoresis bovine proteomics LC-MS/MS sample preparation |
| url | https://www.mdpi.com/2304-8158/8/2/60 |
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