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Amino acid sequence of bovine osteoinductive factor
H Bentz1, R J Chang, A Y Thompson
1Celtrix Laboratories, Collagen Corporation, Palo Alto, California 94303.
The Journal of Biological Chemistry
|March 25, 1990
Summary
The complete amino acid sequence of bovine osteoinductive factor (OIF) was determined. This protein has 105 residues, two cysteines, and two glycosylation sites, with no known homology to other proteins.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Chemistry
Background:
- Osteoinductive factors (OIF) are crucial for bone formation.
- Understanding the primary structure of OIF is essential for elucidating its function and mechanism of action.
Purpose of the Study:
- To determine the complete amino acid sequence of bovine osteoinductive factor (OIF).
- To identify key structural features of OIF, including disulfide bonds and glycosylation sites.
Main Methods:
- Automated Edman degradation was employed for sequence determination.
- Enzymatic cleavage with endoproteinases Lys-C, Glu-C, and Asp-N was used to generate fragments.
- Peptide profiles of native and deglycosylated OIF were compared to identify glycosylation sites.
Main Results:
- The complete amino acid sequence of bovine OIF, comprising 105 residues, was established.
- A molecular weight of 12,055 was calculated for OIF.
- Two intramolecularly linked cysteines (residues 62 and 95) and two asparagine-linked glycosylation sites (positions 52 and 65) were identified.
- Bovine OIF sequence showed no homology to other known proteins.
Conclusions:
- The primary structure of bovine OIF has been fully elucidated.
- Key structural elements, including disulfide bridges and glycosylation, were identified.
- The unique sequence of OIF suggests a novel protein family involved in osteoinduction.