Journal of Analytical & Bioanalytical Techniques
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A relatively small number of well-characterized inhibitors of kidney stone formation
have been identified from the previous research involved in its formation. In this
study conventional biochemical methods have been combined with recent advances
in mass spectrometry (MS) to identify a novel calcium oxalate (CaOx) crystal growth
inhibitor in human renal stone matrix. Proteins were isolated from the matrix of
human CaOx containing kidney stones. Proteins having MW>10 kDa were subjected
to anion exchange and molecular-sieve chromatography. Protein fractions were
tested for their effects on CaOx crystal growth. Most potent fraction was excised, in-
gel tryptic digested and identified by matrix assisted laser desorption/ionization-time
of flight (MALDI-TOF) MS. An anionic protein (MW~42 kDa) with potent inhibitory
activity against CaOx crystal growth was purified. Its homogeneity was confirmed
by RP-HPLC. It was identified by MALDI-TOF-MS followed by database search
on MASCOT server as human phosphate cytidylyltransferase 1, beta. Molecular
weight of this novel CaOx crystal growth inhibitor from human renal stone matrix
is also the same as that of human phosphate cytidylyltransferase 1, choline, beta.
Human phosphate cytidylyltransferase 1, choline, beta is a novel CaOx crystal
growth inhibitor. It is involved in the biosynthesis of phosphatidylcholine which
happens to be an important constituent of human renal stones and is also reported
to have an antilithiatic effect.
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