INTERACTION OF THE CYCLOPHOSPHAMIDE METABOLITE, ACROLEIN, WITH LACTATE DEHYDROGENASE-M HOMOLOG
- Authors:
- Published online on: April 1, 1993 https://doi.org/10.3892/ijo.2.4.683
- Pages: 683-693
Metrics: Total
Views: 0 (Spandidos Publications: | PMC Statistics: )
Total PDF Downloads: 0 (Spandidos Publications: | PMC Statistics: )
Abstract
The cyclophosphamide metabolite, acrolein, binds to both nucleic acids and proteins. In this report, acrolein is shown to interact preferentially with a rat liver 35KD DNA-binding protein. The 35KD protein was purified to homogeneity from a hepatic microsomal fraction using (NH4)2SO4 precipitation, DEAE-Sepharose chromatography, cation exchange HPLC, and DNA-Sepharose affinity chromatography. The protein was identified as a homologue of lactate dehydrogenase (LDH) M subunit on the basis of partial amino acid sequencing, amino acid composition and immunological methods. The interaction of this protein with acrolein may have implications for tissue-specific toxicities and/or oncoselectivity of cyclophosphamide.
