| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10540728 | Food Chemistry | 2006 | 8 Pages |
Abstract
⺠The protein phosphorylation of pork myofibril proteins was analysed using a novel gel-based phosphoproteomic approach. ⺠The global phosphorylation level showed reverse change patterns between fast and slow pH decline rate group. ⺠35 unique proteins were identified, including 11 phosphoproteins. ⺠The phosphorylation patterns of several proteins were significantly (p < 0.05) affected by PM time and pH decline rate. ⺠Our results indicated the role of protein phosphorylation on meat rigor mortis and quality development.
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Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Honggang Huang, Martin R. Larsen, René Lametsch,