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Identification of Ricin in Crude and Purified Extracts From Castor Beans Using On-Target Tryptic Digestion and MALDI Mass Spectrometry

Identification of Ricin in Crude and Purified Extracts From Castor Beans Using On-Target Tryptic Digestion and MALDI Mass Spectrometry

Craig S Brinkworth

Anal Chem. 2010 Jun 15;82(12):5246-52.

PMID: 20486671

Abstract:

Ricin is a toxic protein produced in the seeds of the castor bean plant. The toxicity of the protein and the ease in which it can be extracted from the seeds makes it a potential biological warfare agent. There has been extensive work in the development of analytical techniques that can identify the protein robustly and rapidly. On-target tryptic digestion and MALDI MS was used to distinguish ricin from bovine serum albumin and three other type 2 ribsome-inactivating proteins (RIPs), abrin, agglutinin (RCA(120)), and viscumin, using the peptide mass fingerprint. The sequence coverage obtained was enhanced using methanol-assisted tryptic digestion and was particularly useful for the detection of these toxins in complex matrixes. When used in conjunction with intact protein MALDI mass measurement, a positive identification of ricin (or any of the other RIPs) was achieved including confirmation of the integrity of the disulfide bond between the A and B chains. This applicability of this methodology was demonstrated by the identification of ricin in a typical "crude white powder" that may be illicitly produced in a clandestine lab. The analysis on the solubilized sample using this method can be undertaken in around an hour with minimal sample preparation.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42417980	Lectin from Ricinus communis (castor bean) Agglutinin RCA120			Price

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