Corpus ID: 33559148

Protein cross-linking properties of the antitumor agent inosine dialdehyde (NSC-118994).

  title={Protein cross-linking properties of the antitumor agent inosine dialdehyde (NSC-118994).},
  author={R. Cysyk and R. Adamson},
  journal={Cancer treatment reports},
  volume={60 5},
Inosine dialdehyde (IdA), a new antitumor agent presently undergoing clinical evaluation in man, possesses two aldehyde groups that form stable complexes with a variety of biologic molecules containing amino groups. Complex formation of IdA with lysine, glycine, histidine, or bovine serum albumin (BSA) greatly reduces the cytotoxicity of IdA against L1210 leukemia in vitro. Complexes of IdA and BSA exhibit molecular weights ranging from 69,000 to greater than 800,000 as determined by Sephadex G… Expand
Antiproliferative activity of purine nucleoside dialdehydes against leukemia L1210 in vitro
The most interesting agent in this group of compounds was the lipophilic nucleoside dialdehydes obtained from N6-benzyladenosine after periodate oxidation, and appears to function by limiting the formation of deoxyguanosine diphosphate by inhibition of ribonucleoside diph phosphate reductase, the rate limiting step in the biosynthesis of de oxygenribonucleotides. Expand
An explanation for nonimmunologic adsorption of proteins onto red blood cells: Schiff's base reactions.
In vitro studies with INOX and glutaraldehyde showed nonimmunologic adsorption of protein onto red cells, probably by the condensation of aldehyde groups of these compounds to form Schiff's bases with amino acids of serum proteins and red cell membrane proteins, which provides an explanation for the globulin detected on the red cells of patients treated with InOX. Expand
Inhibition of RNA synthesis in Ehrlich tumor cells by the dialdehyde derivative of inosine (NSC 118994).
The inhibition ofRNA synthesis in the nuclei from INOX-treated cells was completely reversed by the addition of exogenous polydeoxyadenylate-deoxythymidylate as template, showing that the inhibition of RNA synthesis by INOX was not due to the inhibitionof RNA polymerases but rather was due to chain termination of the growing RNA strand or impairment of template function. Expand