Isolation and characterization of two novel calcium-dependent phospholipid-binding proteins from bovine lung

Two calcium-dependent proteins of apparent M r 32000 and 34000 were isolated from bovine lung. Approx. 70 mg/kg of each was obtained. Two-dimensional gel electrophoresis in the presence of 8 M urea showed their apparent p I values to be 5.1 and 5.0, respectively. Both proteins are related immunologi...

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Bibliographic Details
Published in:FEBS letters 1988-06, Vol.233 (2), p.233-238
Main Authors: Boustead, Catherine M., Walker, John H., Geisow, Michael J.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Annexin
Bovine lung
Ca 2+-dependent phospholipid-binding protein
Ca2+-dependent phospholipid-binding protein
Calcium
calcium-dependent phospholipid-binding proteins
Calpactin
Carrier Proteins - isolation & purification
Carrier Proteins - metabolism
Cattle
Chromatography, DEAE-Cellulose
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Endonexin
gel electrophoresis
Lipocortin
Lung - metabolism
Molecular Sequence Data
Molecular Weight
Phospholipids - metabolism
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Summary:Two calcium-dependent proteins of apparent M r 32000 and 34000 were isolated from bovine lung. Approx. 70 mg/kg of each was obtained. Two-dimensional gel electrophoresis in the presence of 8 M urea showed their apparent p I values to be 5.1 and 5.0, respectively. Both proteins are related immunologically to calelectrin from Torpedo marmorata. They also have very similar amino acid compositions to calelectrin. Partial sequence information shows that both proteins contain the highly conserved sequence described for the annexins, a new family of calcium-dependent membrane-binding proteins. In common with other members of this family, the new proteins bind to acidic phospholipids in a calcium-dependent manner.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(88)80433-2