Isolation and characterization of two novel calcium-dependent phospholipid-binding proteins from bovine lung.
Two calcium-dependent proteins of apparent Mr 32,000 and 34,000 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/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.
Boustead
C M
CM
Department of Biochemistry, University of Leeds, England.
Walker
J H
JH
Geisow
M J
MJ
D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002417:Cattle; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008168:Lung / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010743:Phospholipids / Q000378:metabolism*
D002352:Carrier Proteins; D010743:Phospholipids; D002118:Calcium