Amino acids of ricin and its polypeptides

  title={Amino acids of ricin and its polypeptides},
  author={Srinivas V. S. Chakravartula and Nagaraj Guttarla},
  journal={Natural Product Research},
  pages={258 - 263}
Ricin and its corresponding polypeptides (A & B chain) were purified from castor seed. The molecular weight of ricin subunits were 29,000 and 28,000 daltons. The amino acids in ricin determined were Asp45 The22 Ser40 Glu53 Cys4 Gly96 His5 Ile21 Leu33 Lys20 Met4 Phe13 Pro37 Tyr11 Ala45 Val23 Arg20 indicating that ricin contains approximately 516 amino acid residues. The amino acids of the two subunits of ricin A and B chains were Asp23 The12 Ser21 Glu29 Cys2 Gly48 His3 Ile12, Leu17 Lys10 Met2… 
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Determination and Purification of Ricin Protein from Ricinus communis L. Seeds using CLC (Column Liquid Chramotagoraphy) and FPLC (Fast Protein Liquid Chramatography)
The Bradford method was used to quantify purified ricin, and the fractions obtained from FPLC were higher than those obtained from CLC, which might contribute to understanding the chemical properties of the ricin protein from R. communis L. seeds.
Electrochemical study of ricin at glassy carbon electrode.
Electrochemical oxidation of RCA 60 on a glassy carbon (GC) electrode over a wide pH range is studied, using cyclic voltammetry, differential pulsevoltammetry (DPV) and square wave voltAMmetry (SWV) to develop an analytical voltammetric method.


The primary sequence of Ricinus communis agglutinin. Comparison with ricin.
A mixture of synthetic oligonucleotides representing all possible sequences of a peptide present in the ricin B chain has been used to screen a cDNA library constructed using ripening castor bean seed poly(A+) RNA and demonstrated that two classes were present representing sequences complementary to two distinct but closely related preprolectin mRNA species.
The three-dimensional structure of ricin at 2.8 A.
Purification and Physicochemical Properties of Ricins and Agglutinins from Ricinus communis
Two toxin ricins and two agglutinins have been purified from the seeds of Ricinus communis by an improved procedure based on ion-exchange chromatography and gel filtration. One of the two purified
Techniques in Protein Chemistry
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