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. Author manuscript; available in PMC: 2010 Nov 22.
Published in final edited form as: J Proteomics Bioinform. 2010 Jun 1;3(6):191–199. doi: 10.4172/jpb.1000139

Table 2.

Identification of candidate biomarkers obesity and diabetes1.

Protein Name2 Protein MW (Da)3 Protein
pI4
MS/MS Search
Score5
Distinct Peptides6 Spectral Intensity (×107) for respective patients
ID7
1-A 3-B 5-C 8-D
Apolipoprotein B precursor 515533.1 6.58 640.05 49 5.96 16.8 17.2 4.20
Complement component 4A 192788.6 6.72 298.16 21 22.3 25.5 21.0 4.99
Ceruloplasmin 123002.7 5.46 281.99 19 35.1 27.7 51.3 9.77
Fibronectin 1 272337.8 5.3 210.73 16 4.83 6.28 11.9 1.71
Inter-alpha-trypsin inhibitor family heavy chain-related protein 103385.9 6.51 153.9 11 40.6 33.2 29.9 4.53
Inter-alpha inhibitor H1 101366.7 6.43 143.71 10 8.85 13.5 9.96 3.81
Hemopexin 51676.7 6.55 140.64 9 39.3 61.8 48.2 18.6
Apolipoprotein A-1 preproprotein 30778 5.56 117.16 7 3.33 39.3 27.9 11.7
Beta-2-glycoprotein 1 apolipoprotein H 38312.5 8.34 101.84 7 87.9 41.2 70.6 6.05
Alpha-1B-glycoprotein precursor 54272.8 5.58 100.81 7 26.9 32.3 34.1 7.33
Angiotensinogen precursor variant 53778.2 5.97 87.81 6 36.9 36.8 71.6 6.26
1

LC-MS/MS Spectrum Mill database-search for plasma samples obtained from control obese and/or diabetic patients.

2

List of the protein.

3

Theoretical MW (Da) of the identified protein from the database.

4

Theoretical isolelectric points (pI) of the identified protein from the database.

5

MS/MS search score is computed by scoring function that measure the degree of similarity between the experimental spectrum and the theoretical fragmentation patterns of the candidate peptides.

6

Number of the distinct peptides of the protein after fragmentation and is based on the homology of the protein with the known protein in the database.

7

The intensity fold increase of the spectra in the sample is calculated by the factor 1×107.