Table 5 Extent of two glycosylation forms of hydroxylysine in type I collagen isolated from MC and KO clone.
From: Lysyl hydroxylase 2 mediated collagen post-translational modifications and functional outcomes
| Â | Â | Site occupancy (%) | ||||
|---|---|---|---|---|---|---|
MC | EV | KO-1 | KO-2 | KO-3 | ||
α1(I) K87 | G-Hyl | 8.2 ± 0.2 | 8.2 ± 0.2 | 12.8 ± 0.4***,### | 12.6 ± 0.5***,### | 8.0 ± 0.9 |
GG-Hyl | 91.8 ± 0.2 | 91.8 ± 0.2 | 87.2 ± 0.4***,### | 87.4 ± 0.5***,### | 92.0 ± 0.9 | |
α1(I) K99 | G-Hyl | 64.9 ± 1.0 | 65.5 ± 0.5 | 73.2 ± 0.6***,### | 72.3 ± 1.1***,### | 63.9 ± 0.6 |
GG-Hyl | 35.1 ± 1.0 | 34.5 ± 0.8 | 26.8 ± 0.6***,### | 27.7 ± 1.1***,### | 36.1 ± 0.6 | |
α1(I) K174 | G-Hyl | 56.8 ± 1.5 | 56.8 ± 2.2 | 73.0 ± 1.1***,### | 71.5 ± 2.3***,### | 65.8 ± 0.7***,### |
GG-Hyl | 43.2 ± 1.5 | 43.2 ± 2.2 | 27.0 ± 1.1***,### | 28.5 ± 2.3***,### | 34.2 ± 0.7***,### | |
α1(I) K564 | G-Hyl | 47.1 ± 1.4 | 48.9 ± 2.6 | 63.0 ± 1.8***,### | 64.0 ± 3.5***,### | 58.2 ± 1.2***,## |
GG-Hyl | 52.9 ± 1.4 | 51.1 ± 2.6 | 37.0 ± 1.8***,### | 36.0 ± 3.5***,### | 41.8 ± 1.2***,## | |
α2(I) K174 | G-Hyl | 65.3 ± 1.7 | 65.7 ± 0.5 | 76.5 ± 0.6***,### | 75.1 ± 0.8***,### | 63.8 ± 0.8 |
GG-Hyl | 34.7 ± 1.7 | 34.3 ± 0.5 | 23.5 ± 0.6***,### | 24.9 ± 0.8***,### | 36.2 ± 0.8 | |
α2(I) K219 | G-Hyl | 14.8 ± 4.5 | 18.6 ± 0.5 | 27.4 ± 5.5* | 23.5 ± 4.7 | 16.5 ± 1.8 |
GG-Hyl | 85.2 ± 4.5 | 81.4 ± 0.5 | 72.6 ± 5.5* | 76.5 ± 4.7 | 83.5 ± 1.8 | |