Studies on propylamine transfer activity in anti-AdoDATO antibodies

G. Pontoni, L. Lopalco, S. De Maria, U. Zambardino, M. Cartenì-Farina, A. G. Siccardi, V. Zappia

Research output: Contribution to journalArticlepeer-review


Based on a structural similarity to the transition state of a propylamine transfer reaction involved in polyamine biosynthesis, S-adenosyl-(5')-1,8-diamino-3-thiooctane (AdoDATO), the most potent inhibitor of spermidine synthases, was used as a hapten for mice immunization. From immunized mice sera, the IgG fractions were purified by means of affinity (protein A/G) chromatography. Sera and purified polyclonal antibodies from several mice were found to exert spermidine synthase-like activity. Moreover, by means of hybridoma technology, 19 anti-AdoDATO hybridoma clones have been screened for propylamine transfer activity and at least 6 were found to produce catalytic antibodies. These findings indicate the presence in the sera of active spermidine synthase-like catalytic antibodies. The reported results for the first time evidence the feasibility of preparation of N-alkylating antibodies, widening the biotechnological perspectives of antibodies as biocatalysts.

Original languageEnglish
Pages (from-to)299-308
Number of pages10
JournalAmino Acids
Issue number3-4
Publication statusPublished - 1997


  • Amino acids
  • Aminopropyl transferase
  • Catalytic antibodies
  • Polyamines
  • Transition state analogs

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry
  • Endocrinology


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