Phosphoproteomics analysis of postmortem porcine muscle with pH decline rate and time difference

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Phosphoproteomics analysis of postmortem porcine muscle with pH decline rate and time difference. / Huang, Honggang; Larsen, Martin R; Karlsson, Anders H; Lametsch, Rene.

In: International Congress on Meat Science and Technology. Proceedings, 2012.

Research output: Contribution to journalConference articleResearchpeer-review

Harvard

Huang, H, Larsen, MR, Karlsson, AH & Lametsch, R 2012, 'Phosphoproteomics analysis of postmortem porcine muscle with pH decline rate and time difference', International Congress on Meat Science and Technology. Proceedings.

APA

Huang, H., Larsen, M. R., Karlsson, A. H., & Lametsch, R. (2012). Phosphoproteomics analysis of postmortem porcine muscle with pH decline rate and time difference. International Congress on Meat Science and Technology. Proceedings.

Vancouver

Huang H, Larsen MR, Karlsson AH, Lametsch R. Phosphoproteomics analysis of postmortem porcine muscle with pH decline rate and time difference. International Congress on Meat Science and Technology. Proceedings. 2012.

Author

Huang, Honggang ; Larsen, Martin R ; Karlsson, Anders H ; Lametsch, Rene. / Phosphoproteomics analysis of postmortem porcine muscle with pH decline rate and time difference. In: International Congress on Meat Science and Technology. Proceedings. 2012.

Bibtex

@inproceedings{4e1c874c88a540ca895fb583d246f2b3,
title = "Phosphoproteomics analysis of postmortem porcine muscle with pH decline rate and time difference",
abstract = "The aim of this study was to characterize the protein phosphorylation in postmortem (PM) muscle and reveal the change during meat quality development. The gel-based phosphoproteomic analysis of PM porcine muscle was performed in three pig groups with different pH decline rates from PM 1h to 24 h. The sarcoplasmic and myofibrillar fractions were analyzed using gel electrophoresis in combination with a phosphoprotein specific staining. Globally, the group with fast pH decline rate had the highest phosphorylation level at PM 1 h, but lowest at PM 24 h, whereas the group with slow pH decline rate showed the reverse case. The phosphorylation level of 12 bands in sarcoplasmic fraction and 3 bands in myofibrillar fraction were significantly affected by the synergy effects of pH and time (p<0.05). 72 unique proteins were identified. The phosphorylation patterns of pyruvate kinase, triosephosphate isomerase-1, tropomyosin and myosin regulatory light chain 2 showed to be related to PM muscle pH decline rate and time. Our work sheds light on the potential role of protein phosphorylation on regulation of meat quality development.",
author = "Honggang Huang and Larsen, {Martin R} and Karlsson, {Anders H} and Rene Lametsch",
year = "2012",
language = "English",
journal = "International Congress on Meat Science and Technology. Proceedings",
issn = "1025-904X",

}

RIS

TY - GEN

T1 - Phosphoproteomics analysis of postmortem porcine muscle with pH decline rate and time difference

AU - Huang, Honggang

AU - Larsen, Martin R

AU - Karlsson, Anders H

AU - Lametsch, Rene

PY - 2012

Y1 - 2012

N2 - The aim of this study was to characterize the protein phosphorylation in postmortem (PM) muscle and reveal the change during meat quality development. The gel-based phosphoproteomic analysis of PM porcine muscle was performed in three pig groups with different pH decline rates from PM 1h to 24 h. The sarcoplasmic and myofibrillar fractions were analyzed using gel electrophoresis in combination with a phosphoprotein specific staining. Globally, the group with fast pH decline rate had the highest phosphorylation level at PM 1 h, but lowest at PM 24 h, whereas the group with slow pH decline rate showed the reverse case. The phosphorylation level of 12 bands in sarcoplasmic fraction and 3 bands in myofibrillar fraction were significantly affected by the synergy effects of pH and time (p<0.05). 72 unique proteins were identified. The phosphorylation patterns of pyruvate kinase, triosephosphate isomerase-1, tropomyosin and myosin regulatory light chain 2 showed to be related to PM muscle pH decline rate and time. Our work sheds light on the potential role of protein phosphorylation on regulation of meat quality development.

AB - The aim of this study was to characterize the protein phosphorylation in postmortem (PM) muscle and reveal the change during meat quality development. The gel-based phosphoproteomic analysis of PM porcine muscle was performed in three pig groups with different pH decline rates from PM 1h to 24 h. The sarcoplasmic and myofibrillar fractions were analyzed using gel electrophoresis in combination with a phosphoprotein specific staining. Globally, the group with fast pH decline rate had the highest phosphorylation level at PM 1 h, but lowest at PM 24 h, whereas the group with slow pH decline rate showed the reverse case. The phosphorylation level of 12 bands in sarcoplasmic fraction and 3 bands in myofibrillar fraction were significantly affected by the synergy effects of pH and time (p<0.05). 72 unique proteins were identified. The phosphorylation patterns of pyruvate kinase, triosephosphate isomerase-1, tropomyosin and myosin regulatory light chain 2 showed to be related to PM muscle pH decline rate and time. Our work sheds light on the potential role of protein phosphorylation on regulation of meat quality development.

M3 - Conference article

JO - International Congress on Meat Science and Technology. Proceedings

JF - International Congress on Meat Science and Technology. Proceedings

SN - 1025-904X

ER -

ID: 37928078