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. Author manuscript; available in PMC: 2012 Oct 3.
Published in final edited form as: Proteomics. 2011 Nov 23;11(24):4660–4676. doi: 10.1002/pmic.201100058

Table 5.

Identification of proteins from cell surface or cellular location with affinity for α1(XI)NTD by affinity chromatography-mass spectrometry.

Protein namea Common
Abbreviationb
Mr Pred.c
(kDa)
Mr Experimentald
(kDa)
Peptide Matchese Seq.cov.(%)f
Cell Surface Location

Annexin I ANXA1 29.1 35, 32 9 39
Annexin II ANXA2 49.4 38,35,32 14 40
Annexin V ANXA5 36.1 35 16 62
Calreticulin (GRP60) CALR 48 55 6 18
Nucleolin NUCL 77.4 100 10 13

Protein Fate and Modification

Procollagen -lysine, 2-oxoglutarate 5-dioxygenase 1 PLOD1 83.5 75 8 16
Protein disulfide isomerase A3 PDIA3 56.7 60,55 17 39
Protein Disulfide Isomerase A4 PDIA4 72.5 75 8 18
Heat shock 70kDa protein 5(GRP78) HSPA5 72.3 75 8 18
Tumor rejection antigen (gp96 or HSP90B1) HSP90B1 92.4 100 6 9

Metabolic, cytoskeletal, and nuclear proteins

Fructose Bisphophate Aldolase ALDOA 39.5 45,38 10 30
Serotransferrin TF 77.8 75 8 12
Lactate dehydrogenase A LDHA 36.6 32, 35 9 31
Actin, beta ACTB 42 29 13 45
Alpha-actinin 4 ACTN4 104.8 100 9 15
Acidic leucine-rich nuclear phosphoprotein 32 family member B ANP32B 29.9 32 5 15
a

Full name of reference sequence;

b

Common protein abbreviation;

c

Predicted Mr according to NCBI;

d

Experimental Mr calculated by analysis of gel images;

e

Number of peptide matches corresponding to the reference sequence;

f

Sequence coverage calculated as the number of amino acids identified of the total number of amino acids in reference sequence.