Proteome changes underpin improved meat quality and yield of chickens (Gallus gallus) fed the probiotic Enterococcus faecium

Zheng, Aijuan; Luo, Jianjie; Meng, Kun; Li, Jianke; Zhang, Shu; Li, Ke; Liu, Guohua; Cai, Huiyi; Bryden, Wayne L; Yao, Bin

doi:10.1186/1471-2164-15-1167

Table 2 Differential proteins classified by biological process in the pectoral muscles of 42-day-old AA broiler chickens fed the dietary probiotic E. faecium ^a

From: Proteome changes underpin improved meat quality and yield of chickens (Gallus gallus) fed the probiotic Enterococcus faecium

Spot no.	Protein name	Accession no.	Symbol ID	Mr (kDa)/pI	Sequence coverage (%)	Matched	Mascot score	Av. ratio	pvalue
Carbohydrate and energy metabolism
7	Phosphoglucomutase-1 (EC = 5.4.2.2)	gi\|84619526	PGM1	67.063/8.98	40	49	851	1.7	2.60E − 04
12	L-lactate dehydrogenase A chain (EC = 1.1.1.27)	gi\|45384208	LDHA	36.776/7.75	48	30	542	1.7	2.40E − 03
13	Mitochondrial creatine kinase (EC = 2.7.3.2)	gi\|268370038	CKMT2	45.851/8.72	28	10	169	2.0	4.20E − 03
14	Pyruvate kinase muscle isozyme (EC = 2.7.1.40)	gi\|45382651	PKM2	58.434/7.29	18	22	206	−1.5	1.70E − 04
15	Creatine kinase M-type (EC = 2.7.3.2)	gi\|45382875	CKM	43.529/6.50	16	16	75	1.8	1.90E − 04
17	Fructose-1,6-bisphosphatase 2 (EC = 3.1.3.11)	gi\|50762391	FBP2	37.364/8.09	35	25	621	1.7	2.60E − 03
18	β-Enolase (EC = 4.2.1.11)	gi\|46048765	ENO3	47.566/7.28	21	22	352	−1.5	2.20E − 02
19	Glyceraldehyde-3-phosphate dehydrogenase (EC = 1.2.1.12)	gi\|46048961	GAPDH	35.989/8.71	46	38	557	1.6	2.10E − 03
20	Phosphoglycerate kinase (EC = 2.7.2.3)	gi\|45384486	PGK	45.087/8.31	10	43	94	1.5	1.80E − 02
21	Phosphoglycerate mutase 1 (EC = 3.1.3.13)	gi\|71895985	PGAM1	29.051/7.03	37	9	120	1.7	5.70E − 03
22	Creatine kinase M-type (EC = 2.7.3.2)	gi\|45382875	CKM	43.529/6.50	15	5	103	1.9	1.50E − 02
Cytoskeleton
1	Myosin-3	gi\|165973976	MYH3	223.88/5.65	19	59	1481	1.9	7.10E − 03
2	Myosin, heavy chain 1	gi\|61657934	MYH1	223.746/5.61	12	41	1209	1.8	1.40E − 03
3	Myosin, heavy chain 2, skeletal muscle	gi\|45383668	MYH2	223.716/5.71	14	39	1039	2.0	6.80E − 04
5	α-Actinin-2	gi\|46048687	ACTN2	104.779/5.26	65	63	472	1.9	3.40E − 04
8	Myosin, heavy chain 6	gi\|61657939	MYH6	223.976/5.63	16	62	1288	−1.6	3.30E − 03
9	Myosin, heavy chain 7B, beta	gi\|45383005	SSMHC	88.521/5.33	3	8	66	−1.8	1.40E − 03
10	Myosin, heavy chain 15	gi\|45382109	MYH15	223.804/5.61	2	13	88	−1.6	1.00E − 02
11	Slow myosin heavy chain 1	gi\|363746193	SM1	31.625/5.83	20	43	170	−1.5	4.00E − 04
16	Structural muscle protein titin	gi\|363735918	TTN	243.174/6.97	8	25	424	1.8	1.60E − 03
Chaperone protein
4	Heat shock 70 kDa protein	gi\|55742654	HSP70	70.098/5.66	23	33	798	1.5	7.70E − 04
Transporter
6	Albumin	gi\|45383974	ALB	71.868/5.51	62	59	1481	2.1	2.70E − 05
Housekeeping protein
23	β-actin	gi\|45382927	ACTB	8.315/9.25	46	46	213	1.01	1.90E-01

^aSpot no. corresponds to the number of protein spot in Figure 1. Protein name is given when proteins were identified by LC-Chip ESI-QTOF MS. Accession number is the unique number given to mark the entry of a protein in the database NCBInr. Theoretical molecular weight (Mr) and isoelectric point (pI) of the identified proteins are retrieved from the protein database of NCBInr. Sequence coverage is the ratio of the number of amino acids in every peptide that matches with the mass spectrum divided by the total number of amino acids in the protein sequence. Matched peptide is the number of paring an experimental fragmentation spectrum to a theoretical segment of protein and searched peptide is the total searched peptide. Mascot score is searched against the database NCBInr. Av. ratio and p value are calculated using DeCyder software version 7.0. Av. ratio is the rate of expression abundance of protein in the treatment muscle and the control muscle.

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