|
|||||
|
|
Purification of bone sialoprotein from the medium of the rat osteoblast-like cell line UMR 106-01 BSP |
|
| Authors: | K. P. Mintz R. J. Midura L. W. Fisher |
| Affiliation: | (1) Present address: Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, Vermont, USA;(2) Present address: Department of Orthopaedic Surgery, University of Iowa, Iowa City, Iowa, USA;(3) Bone Research Branch, National Institute of Dental Research, National Institutes of Health, Building 30/106, 20892 Bethesda, MD, USA |
| Abstract: | Summary Bone sialoprotein (BSP) is an integrin-binding, RGD-containing bone matrix glycoprotein that has been shown to support cell attachment of cell in culture. Purification of large amounts of this protein from bone is possible but the methods are tedious and the yield is generally low. The availability of a transformed rat osteoblastic cell line synthesizing BSP has made it possible to isolate quantities of this protein in a non-denatured form for studies on its structure and function as well as cell attachment. This report describes the purification of 1 to 2 milligrams of BSP from a liter of serum-free medium of the rat osteoblast-like cell line UMR 106-01 BSP. |
| Keywords: | Bone sialoprotein (BSP) Integrin-binding protein Purification RGD |
| 本文献已被 SpringerLink 等数据库收录！ | |