Enzymatic toxicogenation of “Activated” cyclophosphamide by 3′–5′ exonucleases View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1983-01

AUTHORS

L. Bielicki, G. Voelcker, H. J. Hohorst

ABSTRACT

3'-5' Exonucleases from various sources were found to toxicogenate 4-hydroxycyclophosphamide ("activated" cyclophosphamide) by splitting the oxazaphosphorinane ring and releasing an alkylating moiety and acrolein. Neither cyclophosphamide (CP) nor the deactivated metabolites of CP, 4-keto-CP and carboxyphosphamide nor 4-(S-ethanol)-sulfido-CP were attacked by 3'-5' exonucleases. DNA polymerases with proofreading activity, such as DNA polymerase I from E. coli or DNA polymerase delta from rabbit bone marrow, exhibited a tenfold higher specific activity with "activated" CP than "plain" 3'-5' phosphodiesterases such as snake venom phosphodiesterase or 3',5'cyclic AMP phosphodiesterase from bovine heart tissue. High levels of toxicogenating activity were estimated in peripheric human lymphocytes and tissues of lymphatic origin, suggesting that enzymatic toxicogenation plays a key role with respect to the cytotoxic specificity of "activated" CP. More... »

PAGES

27-29

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00391828

DOI

http://dx.doi.org/10.1007/bf00391828

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1052681528

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/6300134


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