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The Amino Acid Sequence of a Ribosome-Inactivating Protein From Saponaria Officinalis Seeds

The Amino Acid Sequence of a Ribosome-Inactivating Protein From Saponaria Officinalis Seeds

B Maras, R Ippoliti, E De Luca, E Lendaro, A Bellelli, D Barra, F Bossa, M Brunori

Biochem Int. 1990 Aug;21(5):831-8.

PMID: 2256945

Abstract:

The complete primary structure of saporin SO-6, a ribosome-inactivating protein extracted from Saponaria officinalis seeds, has been determined. The sequence was reconstructed following purification and analysis of peptides obtained after digestion of the protein with different proteolytic agents. The protein is composed of 253 amino acids, corresponding to a molecular weight of 28,621 Da. Comparison of the primary structure of SO-6 with the sequence deduced from cDNA, shows amino acid substitutions in 11 positions, suggesting a tissue-related genetic variability. When the sequence of saporin is compared to those of two related proteins, ricin A chain and trichosanthin, a low degree of similarity (12%) is found; nevertheless some considerations about structure-function relationships and evolution of RIPs are possible.

Chemicals Related in the Paper:

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

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