The primary structure of a cell-binding bone sialoprotein.
Year: 1988
Type: article
Abstract: We have determined the amino acid sequence of rat bone sialoprotein (BSP). The sequence deduced from a 1974-base pair cDNA encodes a protein of 320 residues, including a 16-residues long signal peptide. The mature BSP has a molecular mass of 33,600 and contains predominantly glutamic acid and glycine residues, which constitute 32% of all residues. The glutamic acid residues are typically distributed in clusters of up to 10 consecutive residues. The tissue distribution of BSP mRNA suggests that the protein may be a unique product of cells in bone tissue. BSP contains an Arg-Gly-Asp sequence, which presumably is responsible for its cell binding properties (Oldberg, A., Franzén, A., Heinegård, D., Pierschbacher, M., and Ruoslahti, E. (1988) J. Biol. Chem. 263, 19433-19436).
Source: Journal of Biological Chemistry
Authors: A Oldberg, A Franzén, D Heinegård
Institution: Lund University
Language: English
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1493047535