Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences
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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 journal › Journal article › Research › peer-review
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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