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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.
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Arthritis Research & Therapy

ISSN: 1478-6362

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