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. 2010 Jan;27(1):263–274. doi: 10.1089/neu.2009.1051

Table 3B.

Gel Spots Differentially Phosphorylated after Spinal Cord Injury

Gel spot number and associated protein isoformsa Vol. Ratio SCI Vol. Ratio sham Fold change NCBI acces. no. Seq. cov. (%)b No. of peptides Theoretical MW/pIe Functions
29. Glyceraldehyde-3-phosphate dehydrogenase ↑ 1.23 ± 0.34** 0.56 ± 0.16 2.20 P04797 54 33/– 36/8.4 Glycolytic enzyme
34. Ubiquitin carboxyl-terminal hydrolase isozyme L1 ↑ 1.50 ± 0.66** 0.24 ± 0.14 6.25 Q9R0P9 71 36/– 25/5.1 Deubiquitinating enzyme
27. Cathepsin D precursor ↓ 3.23 ± 1.24* 7.41 ± 3.30 −2.29 P24268 6 –/2 45/6.7 Aspartyl protease
28. Neurofilament light chain ↓ 2.74 ± 0.81* 6.77 ± 3.80 −2.47 P19527†¶ 20 11/1 61/4.6 Axonal cytoskeleton

The volume ratio (Vol. Ratio) of the Pro-Q Diamond and SYPRO Ruby signals (calculated from VolPro-Q/VolSYPRO Ruby) was used to quantify the relative phosphorylation level of each gel spot; Mean Fold Change was calculated from the ratio of SCI/sham; fold decreases were calculated by dividing 1 by the ratio of the injured to sham samples; arefers to the spot numbers in Figure 1; brefers to the total percentage of the sequence covered by peptide mass fingerprinting (PMF); crefers to the number of peptides that match the sequence for PMF; drefers to the number of peptides used to identify a protein by tandem mass spectrometry (MS/MS) (CI% > 95%); erefers to the theoretical molecular weight (MW) and the theoretical isoelectric point (pI); *p < 0.05; **p < 0.01; †Protein Score CI% >95%, ‡Protein Score CI% > 99%; ¶Total Ion Score CI% >99%.