| Autor: |
N L, Huq, A, Tseng, G E, Chapman |
| Rok vydání: |
1987 |
| Předmět: |
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| Zdroj: |
Biochemistry international. 15(2) |
| ISSN: |
0158-5231 |
| Popis: |
Osteocalcin (OC), the major gamma carboxyglutamic acid (Gla)-containing protein of vertebrate bone, has been isolated from bones of the emu (Dromaius novaehollandae) and the primary structure determined by a combination of gas phase N-terminal sequencing of the intact molecule and a proteolytic fragment, and carboxypeptidase Y C-terminal sequencing. Gla residues were located by counting tritium radioactivity in fractions from the N-terminal sequencing of the tritiated/thermally decarboxylated molecule. Emu OC consists of 48 amino acid residues containing 3 Gla residues, and a single disulphide bond. The C-terminal 29 residues are identical to those of the human and sheep OC sequences. Alignment of the N-terminal sequence against those of other OCs reveals greater sequence homology with chicken OC than with mammalian OCs. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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