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Interactions Between Saporin, a Ribosome-Inactivating Protein, and DNA: A Study by Atomic Force Microscopy

Interactions Between Saporin, a Ribosome-Inactivating Protein, and DNA: A Study by Atomic Force Microscopy

A Poma, L Spanò, E Pittaluga, A Tucci, L Palladino, T Limongi

J Microsc. 2005 Jan;217(Pt 1):69-74.

PMID: 15655064

Abstract:

Saporins are enzymes belonging to the PNAG class (polynucleotide: adenosine glycosidase), plant enzymes commonly known as ribosome-inactivating proteins (RIP), as a result of their property of irreversibly damaging eukaryotic ribosomes. Direct imaging with tapping-mode atomic force microscopy (AFM) has been used to study pGEM-4Z plasmid DNA binding to the saporin-SO6 (isoform from Saponaria officinalis seeds). Saporin wrapped the plasmidic DNA, and distribution of the enzyme molecules along the DNA chain was markedly variable; plasmid digested with saporin-SO6 appeared fragmented or topologically modified. The supercoiled DNA strands were cleaved, giving rise to a linearized form and to relaxed forms. Electrophoretic analysis of the effect of standard preparations of saporin-SO6 on pGEM-4S confirmed the presence of DNA strand-cleaving activity.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4246465	Saporin from Saponaria officinalis seeds			Price

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