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Covalent binding of 3H-labeled adriamycin metabolites to bovine serum albumin and microsomal protein is demonstrated in an aerobic incubation system with rat liver and rat heart microsomes, respectively, using exhaustive organic solvent extraction and gel chromatography. Covalent protein binding was dependent on active microsomes, NADPH, and oxygen and was inhibited by reduced glutathione and other sulfhydryl compounds. The anthracycline moiety was spectrophotometrically evidenced in the adriamycin metabolite(s) covalently bound to protein. Thus, enzymatic activation of adriamycin in the heart with consecutive covalent protein binding of reactive adriamycin semiquinone radicals may contribute to adriamycin cardiotoxicity.
M E Scheulen, and
H Kappus, and
A Nienhaus, and
C G Schmidt
September 1980,
Toxicology and applied pharmacology,
M E Scheulen, and
H Kappus, and
A Nienhaus, and
C G Schmidt
June 1977,
International archives of occupational and environmental health,
M E Scheulen, and
H Kappus, and
A Nienhaus, and
C G Schmidt
May 1996,
Drug metabolism and disposition: the biological fate of chemicals,
M E Scheulen, and
H Kappus, and
A Nienhaus, and
C G Schmidt
November 1975,
Biochemical pharmacology,
M E Scheulen, and
H Kappus, and
A Nienhaus, and
C G Schmidt
January 1986,
Advances in experimental medicine and biology,
M E Scheulen, and
H Kappus, and
A Nienhaus, and
C G Schmidt
March 1978,
Chemico-biological interactions,
M E Scheulen, and
H Kappus, and
A Nienhaus, and
C G Schmidt
January 1983,
Drug metabolism and disposition: the biological fate of chemicals,
M E Scheulen, and
H Kappus, and
A Nienhaus, and
C G Schmidt
January 1986,
Carcinogenesis,
M E Scheulen, and
H Kappus, and
A Nienhaus, and
C G Schmidt
January 1986,
Advances in experimental medicine and biology,
M E Scheulen, and
H Kappus, and
A Nienhaus, and
C G Schmidt
October 2016,
Drug metabolism and disposition: the biological fate of chemicals,
