Identification of Two Phosphorylation Motifs in Bovine Osteopontin
β Scribed by E.S. Sorensen; T.E. Petersen
- Book ID
- 115574063
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 317 KB
- Volume
- 198
- Category
- Article
- ISSN
- 0006-291X
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Osteopontin (OPN) is a multiphosphorylated glycoprotein found in bone and other normal and malignant tissues, as well as in the physiological fluids urine and milk. The present study demonstrates that bovine milk osteopontin is phosphorylated at 27 serine residues and 1 threonine residu
## Abstract Osteopontin is a noncollagenous, phosphorylated extracellular glycoprotein, expressed in mineralized and nonmineralized tissues, organs and body fluids. The protein contains an RGD tripeptide cellβbinding motif, and is subjected to a variety of posttranslational modifications that play