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Seed proteins of Ricinus communis. III. Isolation and characterization of the two-component polypeptide chains of acid resins

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Abstract

It has been shown that the acid form of ricin — ricin T — consists of two nonidentical subunits: isoleucine and alanine subunits with molecular weights of 30 and 28 kDa, respectively. The isoelectric points, N- and C-terminal amino acids, and partial amino acid sequences of these subunits have been determined. The two subunits of ricin T have been found to exhibit differences from and similarities to ricins D and E.

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Authors
  1. D. A. Khashimov
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  2. Kh. G. Alimov
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  3. P. Kh. Yuldashev
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Additional information

Institute of the Chemistry of Plant Substances, Uzbek Academy of Sciences, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 6, pp. 887–892, November–December, 1987.

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Khashimov, D.A., Alimov, K.G. & Yuldashev, P.K. Seed proteins of Ricinus communis. III. Isolation and characterization of the two-component polypeptide chains of acid resins. Chem Nat Compd 23, 742–746 (1987). https://doi.org/10.1007/BF00596658

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  • DOI: https://doi.org/10.1007/BF00596658

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