| Autor: |
Sauter, Arnold, Staudenmann, Werner, Hughes, Graham J., Heizmann, Claus W. |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 1/15/95, Vol. 227 Issue 1/2, p97-101, 5p |
| Abstrakt: |
The amino acid sequence of a novel EF-hand Ca2+-binding protein from the abdominal muscle of the crayfish, Orconectes limosus, has been elucidated by tandem mass spectrometry and automated Edman degradation. The name CCBP-23 (23-kDa crustacean Ca2+-binding protein) is proposed. The protein can also exist as a disulfide-linked homodimer. The sequence of the monomeric form spans 200 residues with an acetylated N-terminal Ser and reveals four EF-hand domains. The 174-mass-unit difference between the calculated average molecular mass of 22669.6 Da deduced from file sequence and the obtained electrospray ionization mass spectroscopy (ESI-MS) mass of 22844 Da has not yet been explained. Partial sequence analysis (137 residues) of CCBP-23 from the lobster, Homarus americanus, showed a sequence identity of 74% with the crayfish protein. Homology searches revealed a 44% sequence identity of CCBP-23 from crayfish to calcyphosine, a Ca2+-binding protein from dog thyroidea (Lefort et al., 1989). Although CCBP-23 also shows a 44% identity to R2D5 antigen (Nemoto et al., 1993), we believe that both proteins represent two distinct subgroups within the family of EF-hand proteins. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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