Proteomics-based approach for identification and purification of human phosphate binding apolipoprotein from amniotic fluid.

Abstract

Human amniotic fluid is of both maternal and fetal origin; it protects the fetus and provides the environment for growth and development of the fetus. We used a proteomics-based approach for targeting and purifying human phosphate binding protein, a member of the DING family of proteins from amniotic fluid, using Blue Sepharose CL-6B, DEAE-Sephacel and gel filtration chromatography. The protein had earlier been reported to be serendipitously purified along with PON1 (paraoxonase 1). It was identified using electro-spray-ionization-time-of-flight mass spectrometry and was found to be human phosphate binding protein. Human phosphate binding proteins have been reported to play a role as phosphate scavengers and may have a protective function against phosphate-related disorders, such as atherosclerosis, diabetes and kidney stones.

• Authors: M Alam, M Mahajan, M Raziuddin, T P Singh, S Yadav
• Journal: Genetics and molecular research : GMR (Genet Mol Res) Vol. 8 Issue 3 Pg. 929-37 (Aug 04 2009) ISSN: 1676-5680 [Electronic] Brazil
• PMID: 19731215 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Apolipoproteins
• Peptides
• Phosphate-Binding Proteins

Topics

• Amino Acid Sequence
• Amniotic Fluid (chemistry)
• Apolipoproteins (analysis, chemistry, isolation & purification)
• Chromatography, Ion Exchange
• Electrophoresis, Gel, Two-Dimensional
• Electrophoresis, Polyacrylamide Gel
• Female
• Humans
• Mass Spectrometry
• Molecular Sequence Data
• Peptides (chemistry)
• Phosphate-Binding Proteins (analysis, chemistry, isolation & purification)
• Pregnancy
• Proteomics (methods)
• Rh Isoimmunization
• Spectrophotometry, Ultraviolet