Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Photoacoustic Fourier-transform infrared spectroscopy was used to study phosphoamino acids and phosphoproteins. Using this method, we have found that the spectral properties of phosphate esters depend on the nature of the linkage, pH, and binding of metal ion. At high pH values, dianionic symmetric stretching of phosphotyrosine and phosphoserine occurs at 984 and 974 reciprocal centimeters, respectively. Analysis of the IR bands of bound phosphate in phosvitin at different pH values gives the pKa value for the esterified phosphates. Addition of aluminum ions to phosvitin at different pH values causes a shift in the phosphate band consistent with a direct binding of aluminum ions to the esterified phosphate. The phosphate signal for 40 micrograms of Pepsin (1 P/mole) is detectable by this method.
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PMID:Use of photoacoustic Fourier-transform infrared spectroscopy to study phosphates in proteins. 799 90

Putative phosphopeptides produced from enzyme hydrolysis of phosvitin were identified and characterised using MALDI-TOF/MS. Phosvitin was heat-pretreated and then hydrolysed using pepsin, thermolysin, and trypsin at their optimal pH and temperature conditions with or without partial dephosphorylation. Pepsin and thermolysin were not effective in producing phosphopeptides, but trypsin hydrolysis produced many peptides from phosvitin: 12 peptides, 10 of which were phosphopeptides, were identified from the trypsin hydrolysate. Twelve peptides were also identified from the trypsin hydrolysate of partially dephosphorylated phosvitin, but the phosphate groups remaining with the peptides were much smaller than those from the trypsin hydrolysate of intact phosvitin. This suggested that the phosphopeptides produced from the partially dephosphorylated phosvitin lost most of their phosphate groups during the dephosphorylation step. Therefore, partial dephosphorylation of phosvitin before trypsin hydrolysis may not be always recommendable in producing functional phosphopeptides if the phosphate groups play important roles for their functionalities.
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PMID:Characterisation of phosvitin phosphopeptides using MALDI-TOF mass spectrometry. 2503 54