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.
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.
Yvon
M
M
Laboratoire des Sciences de la Consommation, INRA-CRJ, Jouy-en-Josas, France.
Anglade
P
P
Wal
J M
JM
D000595:Amino Acid Sequence; D044482:Benzeneacetamides; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D008239:Lysine; D008969:Molecular Sequence Data; D010400:Penicillin G / Q000031:analogs & derivatives* / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism; D012694:Serine; D012709:Serum Albumin / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D044482:Benzeneacetamides; D010446:Peptide Fragments; D012709:Serum Albumin; C015026:benzylpenicilloyl G; D012694:Serine; D014357:Trypsin; D008239:Lysine; D010400:Penicillin G