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MeSH Review


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Disease relevance of Abrus


High impact information on Abrus

  • Methotrexate and chlorambucil, each covalently linked to either abrus agglutinin, abrin, ricinus agglutinin, ricin, or concanavalin A, were prepared [4].
  • When galactose or lactose was added to the cultures together with the lectins, the abrus agglutinin and ricin B chain induced thymidine incorporation was strongly reduced [5].
  • The abrus agglutinin induced thymidine incorporation was not demonstrable before 36 to 40 hr and reached its maximum after 2 to 5 days [5].
  • If lactose was added within the first 4 hr of incubation with abrus agglutinin no stimulation was observed [5].
  • Human lymphocyte cultures were incubated with the nontoxic abrus agglutinin and with ricin B chain, and the incorporation of 3H thymidine was measured [5].

Biological context of Abrus

  • The presence of two essential tryptophan residues/molecule was implicated in the binding site of Abrus agglutinin [Patanjali, Swamy, Anantharam, Khan & Surolia (1984) Biochem. J. 217, 773-781] [6].
  • Studies on tryptophan residues of Abrus agglutinin. Stopped-flow kinetics of modification and fluorescence-quenching studies [6].

Anatomical context of Abrus

  • The antihepatotoxic activities of soyasaponin I and kaikasaponin III, triterpenoidal saponins isolated from Abri Herba, the whole plant of Abrus cantoniensis, were studied on liver injury induced by CCl4 in primary cultured rat hepatocytes [7].
  • This study examined the inhibitory effects of a methanol extract of Abrus precatorius seeds on the motility of washed human spermatozoa [8].

Associations of Abrus with chemical compounds

  • The method is accomplished by 45% saturation ammonium sulfate fractionation from a 5% acetic acid extract of the seeds of Abrus precatorius followed by diethylaminoethyl-Sephadex A-50 and Sepharose 4B affinity chromatography [9].
  • Chemical modification studies on Abrus agglutinin. Involvement of tryptophan residues in sugar binding [10].
  • Inhibition of plasma extravasation by abruquinone A, a natural isoflavanquinone isolated from Abrus precatorius [1].
  • Agglutinin protein purified from the seeds of Abrus precatorius has a high antitumour activity and was crystallized at room temperature with polyethylene glycol 8000 as the precipitant [11].
  • A known isoflavanquinone, abruquinone B ( 1), and a new derivative, abruquinone G ( 2), were isolated from the aerial parts of Abrus precatorius [12].

Gene context of Abrus

  • Sequence analysis of this cDNA revealed a striking similarity to the recently cloned NeuAc alpha-2,6-gal/GalNAc-specific S. nigra bark agglutinin I (SNAI) and to the previously sequenced type-2 ribosome-inactivating proteins from Ricinus communis and Abrus precatorius [13].
  • HSM-Tn also reacted well with Helix pomatia lectin (HPL), Wistaria floribunda lectin (WFL) and Abrus precatorius agglutinin (APA) and precipitated in each case over 81% of the lectin nitrogen added [14].
  • CMS coated with CM-NAPGA showed a lectin-mediated specific aggregation phenomenon by addition of Abrus precatorius agglutinin [15].
  • It also precipitated well with Abrus precatorius (APA), Momordica charantia (MCA) and Ricinus communis (RCA1) agglutinins, but poorly with other lectins [16].


  1. Inhibition of plasma extravasation by abruquinone A, a natural isoflavanquinone isolated from Abrus precatorius. Wang, J.P., Hsu, M.F., Chang, L.C., Kuo, J.S., Kuo, S.C. Eur. J. Pharmacol. (1995) [Pubmed]
  2. A sheep hydatid cyst glycoprotein as receptors for three toxic lectins, as well as Abrus precatorius and Ricinus communis agglutinins. Wu, A.M., Song, S.C., Wu, J.H., Pfüller, U., Chow, L.P., Lin, J.Y. Biochim. Biophys. Acta (1995) [Pubmed]
  3. Post-testicular antifertility effects of Abrus precatorius seed extract in albino rats. Sinha, R. Journal of ethnopharmacology. (1990) [Pubmed]
  4. Lectin derivatives of methotrexate and chlorambucil as chemotherapeutic agents. Lin, J.Y., Li, J.S., Tung, T.C. J. Natl. Cancer Inst. (1981) [Pubmed]
  5. Stimulation of human lymphocytes by galactose-specific abrus and ricinus lectins. Closs, O., Saltvedt, E., Olsnes, S. J. Immunol. (1975) [Pubmed]
  6. Studies on tryptophan residues of Abrus agglutinin. Stopped-flow kinetics of modification and fluorescence-quenching studies. Patanjali, S.R., Swamy, M.J., Surolia, A. Biochem. J. (1987) [Pubmed]
  7. Kaikasaponin III and soyasaponin I, major triterpene saponins of Abrus cantoniensis, act on GOT and GPT: influence on transaminase elevation of rat liver cells concomitantly exposed to CCl4 for one hour. Miyao, H., Arao, T., Udayama, M., Kinjo, J., Nohara, T. Planta Med. (1998) [Pubmed]
  8. Sperm antimotility properties of a seed extract of Abrus precatorius. Ratnasooriya, W.D., Amarasekera, A.S., Perera, N.S., Premakumara, G.A. Journal of ethnopharmacology. (1991) [Pubmed]
  9. Purification, properties, and crystallographic data for a principal nontoxic lectin from seeds of Abrus precatorius. Wei, C.H., Koh, C., Pfuderer, P., Einstein, J.R. J. Biol. Chem. (1975) [Pubmed]
  10. Chemical modification studies on Abrus agglutinin. Involvement of tryptophan residues in sugar binding. Patanjali, S.R., Swamy, M.J., Anantharam, V., Khan, M.I., Surolia, A. Biochem. J. (1984) [Pubmed]
  11. Crystallization of agglutinin from the seeds of Abrus precatorius. Panneerselvam, K., Lin, S.C., Liu, C.L., Liaw, Y.C., Lin, J.Y., Lu, T.H. Acta Crystallogr. D Biol. Crystallogr. (2000) [Pubmed]
  12. Antitubercular and antiplasmodial constituents of Abrus precatorius. Limmatvapirat, C., Sirisopanaporn, S., Kittakoop, P. Planta Med. (2004) [Pubmed]
  13. Characterization and molecular cloning of Sambucus nigra agglutinin V (nigrin b), a GalNAc-specific type-2 ribosome-inactivating protein from the bark of elderberry (Sambucus nigra). Van Damme, E.J., Barre, A., Rougé, P., Van Leuven, F., Peumans, W.J. Eur. J. Biochem. (1996) [Pubmed]
  14. Interaction of hamster submaxillary sialyl-Tn and Tn glycoproteins with Gal, GalNAc and GlcNAc specific lectins. Wu, A.M., Shen, F., Herp, A., Wu, J.H. Mol. Immunol. (1994) [Pubmed]
  15. Release behaviour of 5-fluorouracil from chitosan-gel microspheres immobilizing 5-fluorouracil derivative coated with polysaccharides and their cell specific recognition. Ohya, Y., Takei, T., Kobayashi, H., Ouchi, T. Journal of microencapsulation. (1993) [Pubmed]
  16. Characterization of the okra mucilage by interaction with Gal, GalNAc and GlcNAc specific lectins. Wu, A.M., Jiang, Y.J., Hwang, P.Y., Shen, F.S. Biochim. Biophys. Acta (1995) [Pubmed]
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