Jan 4, 1996

Purification and characterization of folate binding proteins from rat placenta

Biochimica Et Biophysica Acta
Maria P da Costa, Sheldon P Rothenberg

Abstract

Rat placenta contains virtually no unsaturated (i.e., apo-form) folate binding protein. However, by lowering the pH of a solubilized membrane preparation of this tissue to 3.5, the endogenous bound folate was dissociated from the protein and adsorbed to charcoal. The apo-form of the folate binding protein thus obtained was purified by affinity chromatography using pteroylglutamic acid covalently coupled to Sepharose 4B. A single protein band with an apparent M(r) of 36,000 was observed by SDS-polyacrylamide gel electrophoresis of the eluate from the affinity matrix. Western blot of this preparation using a rabbit antiserum raised with the affinity eluate also identified a single 36 kDa protein band. However, peptide sequencing of the N-terminal region of the proteins in the affinity eluate established that it contained two homologous proteins. Computer alignment of the first 22 N-terminal amino acids of each rat placental protein with human, bovine milk and mouse folate binding proteins showed 50-64% identical homology and 27% homology when the eight proteins were aligned together. The affinity of both rat proteins is highest for pteroylglutamic acid (Ka = 1.6.10(9) l/mol) lower for N5-methyltetrahydrofolate and substantially l...Continue Reading

Mentioned in this Paper

Phosphoric diester hydrolase
Hormone Receptors, Cell Surface
Placenta
Folr1
5-methyltetrahydrofolate, calcium salt (1: 1), (L-Glu)-isomer
Tetrahydrofolates
Western Blot
Folate
PLCB1
Plcb1

About this Paper

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