Abstract:
:The covalent binding of pyridoxal 5'-phosphate (PLP) to human serum albumin (HSA) is important in the regulation of PLP metabolism. In plasma, PLP is bound to HSA at a single high-affinity and at two or more nonspecific sites. To characterize the primary PLP binding site, HSA was incubated with [3H] PLP, and the Schiff base linkage was reduced with potassium borohydride. Tryptic peptides were purified, and the major labeled peptide was sequenced. Amino acid analysis confirmed a homogeneous peptide Leu-Asp-Glu-Leu-Arg-Asp-Glu-Gly-Xaa-Ala-Ser-Ser-Ala-Lys which corresponds to residues 182-195 of HSA. The data indicate that Lys190 is the primary PLP binding site. This Lys residue is distinct from other sites of covalent adduct formation; namely, the primary sites for nonenzymatic glycosylation (Lys525) and acetylation by aspirin (Lys199).
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Bohney JP,Fonda ML,Feldhoff RCdoi
10.1016/0014-5793(92)80073-pkeywords:
subject
Has Abstractpub_date
1992-02-24 00:00:00pages
266-8issue
2-3eissn
0014-5793issn
1873-3468pii
0014-5793(92)80073-Pjournal_volume
298pub_type
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