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Two calcium-dependent phospholipid- and membrane-binding proteins have been purified from bovine brain. These are termed CaBP33 and CaBP37. Complete sequence analysis has revealed that these two proteins are isoforms of annexin V. Despite an apparent difference of 4 kDa between the two proteins on SDS-PAGE, only two amino-acid substitutions were found. These are, in CaBP33, Ser-36 and Lys-125 and in CaBP37, Thr-36 and Glu-125. This corresponds to a mass difference of 15 Da. This was confirmed by electrospray mass spectrometric analysis. Both isoforms can be phosphorylated substoichiometrically in vitro by protein kinase C at residue Thr-22.

Original publication

DOI

10.1016/0167-4838(92)90040-k

Type

Journal article

Journal

Biochimica et biophysica acta

Publication Date

11/1992

Volume

1160

Pages

76 - 83

Addresses

Laboratory of Protein Structure, National Institute for Medical Research, Mill Hill, London, UK.

Keywords

Animals, Cattle, Rats, Protein Kinase C, Glutamine, Lysine, Threonine, Serine, Annexin A5, Membrane Proteins, Sequence Alignment, Brain Chemistry, Amino Acid Sequence, Phosphorylation, Molecular Sequence Data