Binding of pyridoxal 5'-phosphate to bovine serum albumin and albumin fragments obtained after proteolytic hydrolysis. Localization and nature of the primary PLP binding site.

International Journal of Peptide and Protein Research
M C HilakG A Van Os

Abstract

The binding of pyridoxal 5'-phosphate (PLP) to bovine serum albumin (BSA), and to large BSA fragments obtained after proteolytic hydrolysis, was investigated in order to study the structure of these fragments in relation to the albumin structure itself, and to get information about the PLP binding sites on albumin. From absorbance and circular dichroism spectra, combined with peptide mapping of the tryptic digests of the reduced PLP-protein complexes, it could be concluded that the primary binding site is localized with the NH2-terminal part of the albumin molecule. The COOH-terminal part contains one or more secondary sites. It appeared that in albumin and in the largest NH2-terminal fragment, the environment of the primary binding site is rather apolar in character. However, in the smallest NH2-terminal fragment this site is more exposed to the solvent. This suggests that the part of the peptide chain which is not common in both fragments has a stabilizing effect on the structure around the primary binding site.

References

Jan 1, 1974·International Journal of Peptide and Protein Research·M C HilakG A Van Os
Dec 1, 1972·Archives of Biochemistry and Biophysics·T P King, E M Spencer
Jun 8, 1971·Biochemistry·J A AndersonC J Grandjean
Nov 9, 1970·Biochemical and Biophysical Research Communications·S Shaltiel, M Cortijo
Sep 1, 1969·European Journal of Biochemistry·E Shechter
Mar 15, 1967·Journal of the American Chemical Society·Y Matsushima, A E Martell

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Citations

Feb 1, 2015·Archives of Biochemistry and Biophysics·Mei M WhittakerJames W Whittaker
Jul 1, 1991·Archives of Biochemistry and Biophysics·M L FondaU M Guempel
Aug 28, 2021·International Journal of Molecular Sciences·Vibhor Mishra, Richard J Heath

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