Binding of benzyl penicilloyl to human serum albumin. Evidence for a highly reactive region at the junction of domains 1 and 2 of the albumin molecule

FEBS Lett. 1989 Apr 24;247(2):273-8. doi: 10.1016/0014-5793(89)81351-1.

Abstract

Tryptic digests of fragment C124-298 of penicilloylated serum albumin, obtained from a penicillin-treated patient or prepared by in vitro conjugation, were analyzed by HPLC. Determinations of benzyl penicilloyl groups (BPO) were performed on the different fractions. Three BPO-containing peptides were identified by their amino acid sequence and the bound BPO was located on lysines 190, 195 and 199 and serine 193. These four main BPO-binding sites are all located on a very short region (10 amino acid residues) of the albumin molecule at the junction of domains 1 and 2.

MeSH terms

  • Amino Acid Sequence
  • Benzeneacetamides
  • Binding Sites
  • Chromatography, High Pressure Liquid
  • Humans
  • Lysine
  • Molecular Sequence Data
  • Penicillin G / analogs & derivatives*
  • Penicillin G / metabolism
  • Peptide Fragments / metabolism
  • Serine
  • Serum Albumin / metabolism*
  • Trypsin / metabolism

Substances

  • Benzeneacetamides
  • Peptide Fragments
  • Serum Albumin
  • benzylpenicilloyl G
  • Serine
  • Trypsin
  • Lysine
  • Penicillin G