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Proteoglycans of Adult Bovine Compact Bone
| Content Provider | Scilit |
|---|---|
| Author | Sato, Sadao Rahemtulla, Firoz Prince, Charles W. Tomana, Milan Butler, William T. |
| Copyright Year | 1985 |
| Abstract | Proteoglycans of bovine compact bone were purified by chromatography of the formic acid precipitate of an EDTA extract. The sequential chromatographic steps consisted of gel filtration on Sepharose CL-6B in 4-M guanidine HCl, ion-exchange chromatography on DEAE-Sephacel in 4-M urea and rechromatography on Sepharose CL-6B in 4-M guanidine HCl. The preparation consisted of a relatively small proteoglycan (Kav = 0.4 on Sepharose CL-6B) containing about 40% protein, 21% hexuronic acid, 23% galactosamine and lesser amounts of other monosaccharides. The core protein was shown by gradient NaDodSO4 gel electrophoresis, electrotransfer and immunodetection to be monodispersed with an Mr = 45,000. Analysis of glycopeptides obtained after papain digestion of the proteoglycan and separation from glycosaminoglycan chains by gel chromatography, indicated that both N-linked and O-linked oligosaccharides were present. The glycosaminoglycan chains liberated by papain digestion eluted from Sepharose CL-6B as a broad peak with Kav = 0.50, slightly ahead of the position of elution of bovine nasal cartilage glycosaminoglycans (Kav = 0.52); the bone glycosaminoglycans are thus slightly larger than those from cartilage and smaller than the ones attached to fetal bone proteoglycans. These chains were totally susceptible to chondroitinase AC II, a procedure that yielded unsaturated disaccharides corresponding predominantly to chondroitin-4-sulfate, and to a lesser extent chondroitin-6-sulfate. Antisera raised against adult bone proteoglycans cross-reacted with core protein of bone proteoglycan (obtained after chondroitinase digestion) but not with papain digested proteoglycan. In addition, they cross-reacted with core protein and trypsin-liberated, chondroitin sulfate rich region (AlTAl) derived from cartilage proteoglycans and, to a lesser extent, rat bone proteoglycans. No cross-reactivity could be detected to Smith-degraded cartilage proteoglycans, bone acidic glycoproteins or serum proteins. |
| Related Links | http://www.tandfonline.com/doi/pdf/10.3109/03008208509089844 |
| Ending Page | 75 |
| Page Count | 11 |
| Starting Page | 65 |
| ISSN | 03008207 |
| e-ISSN | 16078438 |
| DOI | 10.3109/03008208509089844 |
| Journal | Connective tissue research |
| Issue Number | 1 |
| Volume Number | 14 |
| Language | English |
| Publisher | Informa UK Limited |
| Publisher Date | 1985-01-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Connective Tissue Research Biochemical Research Protein Proteoglycans Glycosaminoglycans Adult Sulfate Chondroitin Liberated Lesser Papain Digested Proteoglycan |
| Content Type | Text |
| Resource Type | Article |
| Subject | Orthopedics and Sports Medicine Cell Biology Molecular Biology Biochemistry Rheumatology |
