The Purification and Complete Amino Acid Sequence of the 9000-Mr Ca2+-binding Protein from Rat Placenta. Identity with the Vitamin D-dependent Intestinal Ca2+-binding Protein
Overview
Authors
Affiliations
A 9000-Mr Ca2+-binding protein was isolated from rat placenta and purified to homogeneity by h.p.l.c. procedures. The complete amino acid sequence was established for the 78-residue placental protein. A sequence analysis of a minor component of the rat intestinal Ca2+-binding protein (residues 4-78) and a tryptic peptide (residues 55-74), both purified by h.p.l.c., showed both proteins to be identical. Thus this placental 9000-Mr Ca2+-binding protein is the same gene product as the intestinal Ca2+-binding protein whose synthesis is dependent on vitamin D.
Kumar R, Tebben P, Thompson J Arch Biochem Biophys. 2012; 523(1):77-86.
PMID: 22426203 PMC: 3361542. DOI: 10.1016/j.abb.2012.03.003.
Calcium-binding proteins: distribution and implication in mammalian placenta.
Belkacemi L, Simoneau L, Lafond J Endocrine. 2003; 19(1):57-64.
PMID: 12583602 DOI: 10.1385/ENDO:19:1:57.
Hubbard M Biochem J. 1993; 293 ( Pt 1):223-7.
PMID: 8392333 PMC: 1134343. DOI: 10.1042/bj2930223.
A growth-related mRNA in cultured mouse cells encodes a placental calcium binding protein.
Swiergiel J, Linzer D Nucleic Acids Res. 1987; 15(16):6677-90.
PMID: 3628004 PMC: 306131. DOI: 10.1093/nar/15.16.6677.
Darwish H, Krisinger J, Strom M, DeLuca H Proc Natl Acad Sci U S A. 1987; 84(17):6108-11.
PMID: 3476932 PMC: 299017. DOI: 10.1073/pnas.84.17.6108.