| First Author | Schönekess BO | Year | 1997 |
| Journal | Biochem Cell Biol | Volume | 75 |
| Issue | 6 | Pages | 771-5 |
| PubMed ID | 9599666 | Mgi Jnum | J:47172 |
| Mgi Id | MGI:1202690 | Citation | Schonekess BO, et al. (1997) Molecular cloning and expression of avian smooth muscle S100A11 (calgizzarin, S100C). Biochem Cell Biol 75(6):771-5 |
| abstractText | S100A11 (calgizzarin or S100C), a member of the S100 family of Ca(2+)- binding proteins, was first identified in chicken gizzard smooth muscle and subsequently detected in several mammalian species and tissues. We now report the full-length coding sequence of avian smooth muscle S100A11. The cloned nucleotide sequence is 515 bases in length, which includes in-frame start and stop codons and encodes a protein of 101 amino acids. The chicken S100A11 sequence differs from human S100A11 at 25 positions (9 conserved) and is four residues shorter (overall identity 72.4%, similarity 81%). The protein contains two EF hand and conserved hydrophobic residues involved in dimer formation. Cloned avian S100A11 expressed in Escherichia coli and purified by Ca(2+)-dependent hydrophobic interaction chromatography and ion-exchange chromatography was recognized by polyclonal antibodies raised against tissue-purified protein and, like tissue-purified S100A11, bound 45Ca2+ in a gel overlay assay. |
