Abstract:
: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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Graves DJ,Luo Sdoi
10.1006/bbrc.1994.2710subject
Has Abstractpub_date
1994-11-30 00:00:00pages
618-24issue
1eissn
0006-291Xissn
1090-2104pii
S0006291X84727100journal_volume
205pub_type
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