Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences

Research output: Contribution to journalJournal articlepeer-review

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Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences. / Huang, Honggang; Larsen, Martin Røssel; Karlsson, Anders H; Pomponio, Luigi; Costa, Leonardo Nanni; Lametsch, Rene.

In: Proteomics - Practical Proteomics, Vol. 11, No. 20, 2011, p. 4063-4076.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Huang, H, Larsen, MR, Karlsson, AH, Pomponio, L, Costa, LN & Lametsch, R 2011, 'Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences', Proteomics - Practical Proteomics, vol. 11, no. 20, pp. 4063-4076. https://doi.org/10.1002/pmic.201100173

APA

Huang, H., Larsen, M. R., Karlsson, A. H., Pomponio, L., Costa, L. N., & Lametsch, R. (2011). Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences. Proteomics - Practical Proteomics, 11(20), 4063-4076. https://doi.org/10.1002/pmic.201100173

Vancouver

Huang H, Larsen MR, Karlsson AH, Pomponio L, Costa LN, Lametsch R. Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences. Proteomics - Practical Proteomics. 2011;11(20):4063-4076. https://doi.org/10.1002/pmic.201100173

Author

Huang, Honggang ; Larsen, Martin Røssel ; Karlsson, Anders H ; Pomponio, Luigi ; Costa, Leonardo Nanni ; Lametsch, Rene. / Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences. In: Proteomics - Practical Proteomics. 2011 ; Vol. 11, No. 20. pp. 4063-4076.

Bibtex

@article{c2e36d911c204d958dca287c8343a0a5,
title = "Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences",
abstract = "Meat quality development is highly influenced by the pH decline caused by the postmortem (PM) glycolysis. Protein phosphorylation is an important mechanism in regulating the activity of glycometabolic enzymes. Here, a gel-based phosphoproteomic study was performed to analyze the protein phosphorylation in sarcoplasmic proteins from three groups of pigs with different pH decline rates from PM 1 to 24¿h. Globally, the fast pH decline group had the highest phosphorylation level at PM 1¿h, but lowest at 24¿h, whereas the slow pH decline group showed the reverse case. The same pattern was also observed in most individual bands in 1-DE. The protein phosphorylation levels of 12 bands were significantly affected by the synergy effects of pH and time (p",
keywords = "Animals, Diamond, Hydrogen-Ion Concentration, Muscle, Skeletal, Phosphorylation, Postmortem Changes, Proteomics, Quality Control, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Staining and Labeling, Swine, Time Factors",
author = "Honggang Huang and Larsen, {Martin R{\o}ssel} and Karlsson, {Anders H} and Luigi Pomponio and Costa, {Leonardo Nanni} and Rene Lametsch",
note = "Copyright {\textcopyright} 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",
year = "2011",
doi = "10.1002/pmic.201100173",
language = "English",
volume = "11",
pages = "4063--4076",
journal = "Proteomics - Practical Proteomics",
issn = "1862-7595",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "20",

}

RIS

TY - JOUR

T1 - Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences

AU - Huang, Honggang

AU - Larsen, Martin Røssel

AU - Karlsson, Anders H

AU - Pomponio, Luigi

AU - Costa, Leonardo Nanni

AU - Lametsch, Rene

N1 - Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

PY - 2011

Y1 - 2011

N2 - Meat quality development is highly influenced by the pH decline caused by the postmortem (PM) glycolysis. Protein phosphorylation is an important mechanism in regulating the activity of glycometabolic enzymes. Here, a gel-based phosphoproteomic study was performed to analyze the protein phosphorylation in sarcoplasmic proteins from three groups of pigs with different pH decline rates from PM 1 to 24¿h. Globally, the fast pH decline group had the highest phosphorylation level at PM 1¿h, but lowest at 24¿h, whereas the slow pH decline group showed the reverse case. The same pattern was also observed in most individual bands in 1-DE. The protein phosphorylation levels of 12 bands were significantly affected by the synergy effects of pH and time (p

AB - Meat quality development is highly influenced by the pH decline caused by the postmortem (PM) glycolysis. Protein phosphorylation is an important mechanism in regulating the activity of glycometabolic enzymes. Here, a gel-based phosphoproteomic study was performed to analyze the protein phosphorylation in sarcoplasmic proteins from three groups of pigs with different pH decline rates from PM 1 to 24¿h. Globally, the fast pH decline group had the highest phosphorylation level at PM 1¿h, but lowest at 24¿h, whereas the slow pH decline group showed the reverse case. The same pattern was also observed in most individual bands in 1-DE. The protein phosphorylation levels of 12 bands were significantly affected by the synergy effects of pH and time (p

KW - Animals

KW - Diamond

KW - Hydrogen-Ion Concentration

KW - Muscle, Skeletal

KW - Phosphorylation

KW - Postmortem Changes

KW - Proteomics

KW - Quality Control

KW - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

KW - Staining and Labeling

KW - Swine

KW - Time Factors

U2 - 10.1002/pmic.201100173

DO - 10.1002/pmic.201100173

M3 - Journal article

C2 - 21805635

VL - 11

SP - 4063

EP - 4076

JO - Proteomics - Practical Proteomics

JF - Proteomics - Practical Proteomics

SN - 1862-7595

IS - 20

ER -

ID: 37927670