Title
Covalent binding of nitrogen mustards to the cysteine-34 residue in human serum albumin
Author
Noort, D.
Hulst, A.G.
Jansen, R.
Prins Maurits Laboratorium TNO
Publication year
2002
Abstract
Covalent binding of various clinically important nitrogen mustards to the cysteine-34 residue of human serum albumin, in vitro and in vivo, is demonstrated. A rapid method for detection of these adducts is presented, based on liquid chromatography-tandem mass spectrometry analysis of the adducted tripeptide Cys*-Pro-Phe after digestion of the protein with Pronase.
Subject
Toxicology
Adducts
Albumin
Biomonitoring
Chemotherapy
Nitrogen mustards
Tandem mass spectrometry
Chlorambucil
Chlormethine
Chlormethine derivative
Dichlorodiethylamine
Human serum albumin
Phenylalanine
Proline
Pronase
Tripeptide
Amino acid analysis
Controlled study
Covalent bond
Drug protein binding
In vitro study
In vivo study
Liquid chromatography
Tandem mass spectrometry
Binding Sites
Cyclophosphamide
Cysteine
Drug Monitoring
Humans
Mechlorethamine
Melphalan
Nitrogen Mustard Compounds
Protein Binding
Serum Albumin
Mass spectrometry
Matrix-Assisted Laser Desorption-Ionization
Brassicaceae
Chlorambucil, 305-03-3
Cyclophosphamide, 50-18-0
Cysteine, 52-90-4
Mechlorethamine, 51-75-2
Melphalan, 148-82-3
Nitrogen Mustard Compounds
Nornitrogen mustard, 334-22-5
Serum albumin
To reference this document use:
http://resolver.tudelft.nl/uuid:f0047f8e-2256-4bb1-aff3-9f70f9981d14
DOI
https://doi.org/10.1007/s00204-001-0318-2
TNO identifier
236511
ISSN
0340-5761
Source
Archives of Toxicology, 76 (2), 83-88
Document type
article