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Table 1 Absorbance data from FTIRM used to examine levels of proteoglycan and collagen from different cultures

From: Destructive effects of murine arthritogenic antibodies to type II collagen on cartilage explants in vitro

Sample (no. of spectra) Proteoglycan absorbance Amide 1 peakc
  1072 cm-1a 1242 cm-1b Absorbance Location (cm-1)
Interior (40)d 1.34 ± 0.26 1.94 ± 0.17 5.01 ± 0.15 1666
GAD 6 edge (10) 1.14 ± 0.21 1.66 ± 0.20 4.76 ± 0.44 1666
CIIF4 edge (10) 0.85 ± 0.14 1.51 ± 0.15 4.46 ± 0.19 1659
M2139 edge (10) 0.55 ± 0.14 1.25 ± 0.23 4.31 ± 0.19 1651
CIIC1 edge (10) 0.49 ± 0.12 1.42 ± 0.17 4.63 ± 0.41 1659
M2139 + CIIC1 edge 0.37 ± 0.11 0.99 ± 0.19 4.44 ± 0.15 1639
M2139 + CIIC1 middle 0.50 ± 0.14 1.05 ± 0.15 4.48 ± 0.10 1643
CIIC1 F(ab)2 edge (10) 0.40 ± 0.07 1.03 ± 0.17 4.22 ± 0.14 1648
CIIC1 F(ab)2 interior (10) 0.43 ± 0.1 1.12 ± 0.12 4.18 ± 0.14 1644
  1. aAbsorbance from the proteoglycan peak at 1072 cm-1 is representative of sugars. bAbsorbance from the proteoglycan peak at 1242 cm-1 is representative of sulphated glycosaminoglycans. cThe amide 1 peak provides a measure of total protein, predominantly collagen. Note the change in the location of the amide 1 peak in the presence of mAbs to CII, consistent with the change from 1666–1668 cm-1 to 1652–1653 cm-1 observed after heat denaturation of the collagen helix, or collagenase treatment (see text). Results shown are mean ± SD. dTen spectra from the interior of the cartilage treated with the four antibodies were combined.