Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle

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Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle. / Huang, Honggang; Larsen, Martin Røssel; Lametsch, Rene.

In: Food Chemistry, Vol. 134, No. 4, 2012, p. 1999-2006.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Huang, H, Larsen, MR & Lametsch, R 2012, 'Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle', Food Chemistry, vol. 134, no. 4, pp. 1999-2006. https://doi.org/10.1016/j.foodchem.2012.03.132

APA

Huang, H., Larsen, M. R., & Lametsch, R. (2012). Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle. Food Chemistry, 134(4), 1999-2006. https://doi.org/10.1016/j.foodchem.2012.03.132

Vancouver

Huang H, Larsen MR, Lametsch R. Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle. Food Chemistry. 2012;134(4):1999-2006. https://doi.org/10.1016/j.foodchem.2012.03.132

Author

Huang, Honggang ; Larsen, Martin Røssel ; Lametsch, Rene. / Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle. In: Food Chemistry. 2012 ; Vol. 134, No. 4. pp. 1999-2006.

Bibtex

@article{17b6bbe5cbc74b25a6a1483b36bd4ba5,
title = "Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle",
abstract = "A gel-based phosphoproteomic study was performed to investigate the postmortem (PM) changes in protein phosphorylation of the myofibrillar proteins in three groups of pigs with different pH decline rates, from PM 1 h to 24 h. The global phosphorylation level in the group with a fast pH decline rate was higher than that in the slow and intermediate groups at early PM time, but became the lowest at 24 h. The protein phosphorylation level of seven individual protein bands was only significantly (p<0.05) affected by PM time, and two protein bands were subjected to a synergy effect between PM time and pH decline rate. A total of 35 non-redundant highly abundant proteins were identified from 19 protein bands; most of the identified proteins were sarcomeric function-related proteins. Myosin-binding protein C, troponin T, tropomyosin and myosin regulatory light chain 2 were identified in the highly phosphorylated protein bands with the highest scores. The results indicate that the phosphorylation pattern of myofibrillar proteins in PM muscle is mainly changed with PM time, but only to a minor extent influenced by the rate of pH decline, suggesting that the phosphorylation of myofibrillar proteins may be related to the meat rigor mortis and quality development. --------------------------------------------------------------------------------",
author = "Honggang Huang and Larsen, {Martin R{\o}ssel} and Rene Lametsch",
year = "2012",
doi = "10.1016/j.foodchem.2012.03.132",
language = "English",
volume = "134",
pages = "1999--2006",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier",
number = "4",

}

RIS

TY - JOUR

T1 - Changes in phosphorylation of myofibrillar proteins during postmortem development of porcine muscle

AU - Huang, Honggang

AU - Larsen, Martin Røssel

AU - Lametsch, Rene

PY - 2012

Y1 - 2012

N2 - A gel-based phosphoproteomic study was performed to investigate the postmortem (PM) changes in protein phosphorylation of the myofibrillar proteins in three groups of pigs with different pH decline rates, from PM 1 h to 24 h. The global phosphorylation level in the group with a fast pH decline rate was higher than that in the slow and intermediate groups at early PM time, but became the lowest at 24 h. The protein phosphorylation level of seven individual protein bands was only significantly (p<0.05) affected by PM time, and two protein bands were subjected to a synergy effect between PM time and pH decline rate. A total of 35 non-redundant highly abundant proteins were identified from 19 protein bands; most of the identified proteins were sarcomeric function-related proteins. Myosin-binding protein C, troponin T, tropomyosin and myosin regulatory light chain 2 were identified in the highly phosphorylated protein bands with the highest scores. The results indicate that the phosphorylation pattern of myofibrillar proteins in PM muscle is mainly changed with PM time, but only to a minor extent influenced by the rate of pH decline, suggesting that the phosphorylation of myofibrillar proteins may be related to the meat rigor mortis and quality development. --------------------------------------------------------------------------------

AB - A gel-based phosphoproteomic study was performed to investigate the postmortem (PM) changes in protein phosphorylation of the myofibrillar proteins in three groups of pigs with different pH decline rates, from PM 1 h to 24 h. The global phosphorylation level in the group with a fast pH decline rate was higher than that in the slow and intermediate groups at early PM time, but became the lowest at 24 h. The protein phosphorylation level of seven individual protein bands was only significantly (p<0.05) affected by PM time, and two protein bands were subjected to a synergy effect between PM time and pH decline rate. A total of 35 non-redundant highly abundant proteins were identified from 19 protein bands; most of the identified proteins were sarcomeric function-related proteins. Myosin-binding protein C, troponin T, tropomyosin and myosin regulatory light chain 2 were identified in the highly phosphorylated protein bands with the highest scores. The results indicate that the phosphorylation pattern of myofibrillar proteins in PM muscle is mainly changed with PM time, but only to a minor extent influenced by the rate of pH decline, suggesting that the phosphorylation of myofibrillar proteins may be related to the meat rigor mortis and quality development. --------------------------------------------------------------------------------

U2 - 10.1016/j.foodchem.2012.03.132

DO - 10.1016/j.foodchem.2012.03.132

M3 - Journal article

C2 - 23442649

VL - 134

SP - 1999

EP - 2006

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

IS - 4

ER -

ID: 37928026