Covalent binding of nitrogen mustards to the cysteine-34 residue in human serum albumin.
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.
Noort
Daan
D
Department of Chemical Toxicology, TNO Prins Maurits Laboratory, PO Box 45, 2280 AA Rijswijk, The Netherlands. noortd@pml.tno.nl
Hulst
Albert G
AG
Jansen
Rob
R
D001665:Binding Sites; D002699:Chlorambucil / Q000378:metabolism; D003520:Cyclophosphamide / Q000378:metabolism; D003545:Cysteine / Q000378:metabolism*; D016903:Drug Monitoring / Q000379:methods*; D006801:Humans; D066298:In Vitro Techniques; D008466:Mechlorethamine / Q000378:metabolism; D008558:Melphalan / Q000378:metabolism; D009588:Nitrogen Mustard Compounds / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D009588:Nitrogen Mustard Compounds; D012709:Serum Albumin; D002699:Chlorambucil; D008466:Mechlorethamine; D003520:Cyclophosphamide; C004933:nornitrogen mustard; D003545:Cysteine; D008558:Melphalan