Analysis of a 67 kDa lipid-dependent Ca2+-binding protein from avian matrix vesicles revealed amino acid sequences homologous to mammalian annexin VI. PCR methods were used to identify a clone from an avian cDNA library that contained a full length copy of the 67-kDa annexin cDNA. This was restriction mapped, subcloned and sequenced. The cDNA sequence of the open reading frame showed 70 percent identity to that of murine annexin VI; the predicted amino acid sequence, 78 percent identity. There was no homology in the 5’- and 3’-untranslated regions. A plasmid was constructed that overexpresses the intact chicken 67-kDa matrix vesicle annexin in E. coli DH5α in high yield; the physicochemical properties and the amino terminal sequence of the expressed protein exactly matched those of the native protein.
|Original language||English (US)|
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Dec 15 1993|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology