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Studies on the Antitumor Lectins Isolated From the Seeds of Ricinus Communis (Castor Bean)

Studies on the Antitumor Lectins Isolated From the Seeds of Ricinus Communis (Castor Bean)

J Y Lin, S Y Liu

Toxicon. 1986;24(8):757-65.

PMID: 3775791

Abstract:

Three toxic proteins and one agglutinin were purified from the seeds of Ricinus communis by a simple and fast method using Sepharose 4-B affinity chromatography followed by Sephadex G-100 gel filtration. The weakly adsorbed ricins A and B were retarded and eluted with the buffer from the affinity chromatographic column, while ricin C and ricinus agglutinin had to be eluted with 0.1 M galactose. The molecular weights of ricins A, B, and C were about 62,000 and that of ricinus agglutinin was 120,000, estimated by amino acid compositions and SDS gel electrophoresis. They all possessed two non-identical subunits: A and B chains linked by one disulfide bond. Their LD50 values were 4, 28, 14 and 112 micrograms per kg body weight of mice for ricins A, B and C and ricinus agglutinin, respectively. The amino acid compositions of the three toxins and their A and B subunits were very similar, but not identical, while ricinus agglutinin showed a different composition. Ricin A is a newly isolated lectin which has a strong inhibitory effect on the growth of tumor cells. By using cell cultures, it was demonstrated that the tumor cells were more sensitive to lectin than non-transformed cells, and that this could be caused by the higher binding affinity of lectin to tumor cells than to non-transformed cells.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP96638287	Ricin A chain from Ricinus communis (castor bean)		96638-28-7	Price

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