A Ca2+-binding protein was purified from mouse Ehrlich ascites-tumour cells. The protein forms monomers and disulphide-linked dimers, which can be separated by reverse-phase h.p.l.c. A partial amino acid sequence analysis demonstrated that the protein has an EF-hand structure. A striking homology was found to rat and human calcyclin (a member of the S-100 protein family), which is possibly involved in cell-cycle regulation.
Calcium-binding protein from mouse Ehrlich ascites-tumour cells is homologous to human calcyclin
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J Kuźnicki, A Filipek, P E Hunziker, S Huber, C W Heizmann; Calcium-binding protein from mouse Ehrlich ascites-tumour cells is homologous to human calcyclin. Biochem J 1 November 1989; 263 (3): 951–956. doi: https://doi.org/10.1042/bj2630951
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