Table 1.

Corresponding protein spots on a typical gel (Figure 3) identified using mass spectrometry. Both protein spots in locations D and F were identified as IGHG1 proteins. Here, we differentiate the spots at locations D and F with superscript 1 and 2, respectively.

Location	Protein Name	Structure (protein folding)§
A*	Human serum albumin precursor	Multihelical
B*	Human serum albumin	Multihelical
C*	Transferrin	Mixed beta-sheet of 5 strands
D*	IGHG1 Protein1	Unknown
E	Fibrinogen gamma chain	Not a true fold; includes oligomers of shorter identical helices
F	IGHG1 Protein2	Unknown
G	Haptoglobin precursor & Apolipoprotein A-IV precursor	Two α- and two β-chains & Nearly all-beta
H	Apolipoprotein A-I	Tetrameric antiparallel coiled coil, closed in a circuit
I	Immunoglobulin light chain & Immunoglobulin kappa	Sandwich; 7 strands in 2 sheets; greek-key &
J	Serum retinol-binding protein	Unknown
K	Haptoglobin Hp2	Two α- and two β-chains
L	Serum albumin (truncated)	Multihelical

^*Note: Spots A, B, C and D were not included in the quantitative analysis in Figures 5 and 6 since the spots were smeared out and connected with other protein spots.

^§The protein structure was searched under the general protein family, based on using SCOP: Structural Classification of proteins (http://scop.mrc-lmb.cam.ac.uk/scop/).