Purification and characterization of a new member of the S-100 protein family from human placenta.
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Emoto Y, Kobayashi R, Akatsuka H, Hidaka H
Purification and characterization of a new member of the S-100 protein family from human placenta.
Biochem Biophys Res Commun. 1992 Feb 14;182(3):1246-53.
- PubMed ID
- 1540168 [ View in PubMed]
- Abstract
A novel Ca(2+)-binding protein which is termed S-100P was purified from human placenta with a hydrophobic column followed by an anion exchange column and reverse phase high performance liquid chromatography (HPLC). Molecular mass of the protein was 10 kDa according to sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. Using immunoblotting technique, anti-human calcyclin antibodies did not bind to the S-100P. Isoelectric point of S-100P was pI = 4.6. S-100P did not formed disulfide-linked dimer. Calcium binding ability was proved by UV difference spectrometry, urea/alkaline gel electrophoresis, and 45Ca overlay technique. A ninety amino acid sequence of S-100P was determined. It is 49% identical with human S-100 beta, 38% with human calcyclin, and 37% with human cystic fibrosis antigen.