Toxicological studies on plant proteins: A review

Journal of Applied Toxicology

Volumn 32, Issue 6, 2012, Pages 377-386

  Wu, Wenbiao ^a   Sun, Rong ^a  

^a SOUTHWEST UNIVERSITY   (China)

Author keywords

Dangerous proteins; Dietary safety; Heat labile; New sources; Toxicological studies

Indexed keywords

ABRIN; AGGLUTININ; CANATOXIN; CONCANAVALIN A; EBULIN 1; GLIADIN; GLUTEN; GLYCOSIDASE; HEMAGGLUTININ; LANCEOLIN; LECTIN; MODECCIN; PLANT LECTIN; PULCHELLIN; RIBOSOME INACTIVATING PROTEIN; RICIN; SOYATOXIN; STENODACTYLIN; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; VISCUMIN; VOLKENSIN;

ABRUS; CANAVALIA; CELIAC DISEASE; DIET; DIETARY INTAKE; EICHHORNIA CRASSIPES; ENZYME INHIBITION; ENZYME SUBUNIT; FOOD INTAKE; FOOD SAFETY; HUMAN; IMMUNE RESPONSE; LD 50; LUPIN; MOLECULAR WEIGHT; NONHUMAN; PHASEOLUS VULGARIS; PLANT; PLANT LEAF; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; RAPESEED; REVIEW; SOYBEAN; TOXICITY TESTING;

ANIMALS; CONSUMER PRODUCT SAFETY; HUMANS; LETHAL DOSE 50; MOLECULAR WEIGHT; PLANTS, TOXIC; STRUCTURE-ACTIVITY RELATIONSHIP; TOXICITY TESTS; TOXINS, BIOLOGICAL; VEGETABLE PROTEINS;

ANIMALIA; BRASSICA NAPUS VAR. NAPUS; EICHHORNIA CRASSIPES;

EID: 84860235387     PISSN: 0260437X     EISSN: 10991263     Source Type: Journal    
DOI: 10.1002/jat.1780     Document Type: Review

References (121)

1. Anandan S, Anil Kumar GK, Ghosh J, Ramachandra KS. 2008. Effect of different physical and chemical treatments on detoxification of ricin in castor cake. Animal Feed Sci. Technol. 120(1-2): 159-168; doi: 10.1016/j.anifeedsci.2004.10.002.
2. Araújo APU, Castilho PV, Goto LS. 2010. Ribosome-Inactivating Proteins from Abrus pulchellus. In Plant Toxic Proteins, Plant Cell Monographs18, Lord JM, Hartley MR (eds). Springer: Berlin; 133-147. doi: 10.1007/978-3-642-12176-0_7.
3. Audi J, Belson M, Patel M, Schier J, Osterloh J. 2005. Ricin poisoning: a comprehensive review. JAMA 294(18): 2342-2350.
4. Balint GA. 1974. Ricin: the toxic protein of castor oil seeds. Toxicology 2(1): 77-102.
5. Ballerstadt R, Evans C, McNichols R, Gowda A. 2006. Concanavalin A for in vivo glucose sensing: a biotoxicity review. Biosens. Bioelectron. 22: 275-284.
6. Ballester D, Yaiiez E, Garcia R, Erazo S, Lopez F, Haardt E, Cornejo S, Lopez A, Pokniak J, Chichester CO. 1980. Chemical composition, nutritive value, and toxicological evaluation of two species of sweet (Lupine Lupinus albus and Lupinus luteus). J. Agricult. Food Chem. 28(2): 402-405.
7. Ballester DR, Brunser O, Saitúa MT, Egaña JI, Yáñez EO, Owen DF. 1984. Safety evaluation of sweet lupine (Lupinus albus cv. Multolupa). II. Nine-month feeding and multi-generation study in rats. Food Chem. Toxicol. 2(1): 45-48.
8. Barbieri L, Zamboni M, Montanaro L, Sperti S, Stirpe F. 1980. Purification and properties of different forms of modeccin, the toxin of adenia digitata. separation of subunits with inhibitory and lectin acitivity. Biochem. J. 185: 203-210.
9. Barbieri L, Falasca AI, Stirpe F. 1984. Volkensin, the toxin of Adenia volkensii (kilyambiti plant). FEBS Lett. 171(2): 277-279.
10. Barbieri L, Battelli M, Stirpe F. 1993. Ribosome-inactivating protein from plants. Biochim. Biophys. Acta 1154: 237-282.
11. Barbieri L, Valbonesi P, Gorini P, Pession A, Stirpe F. 1996. Polynucleotide: adenosine glycosidase activity of sapori-L1: effect on DNA, RNA and poly (A). Biochem. J. 319: 507-513.
12. Barbieri L, Valbonesi P, Bonora E, Gorini P, Bolognesi A, Stirpe F. 1997. Polynucleotide: adenosine glycosidase activity of ribosome-inactivating proteins: effect on DNA, RNA and poly(A). Nucl. Acids Res. 25: 518-522.
13. Benson S, Olsnes S, Pihl A, Skorve J, Abraham AK. 1975. On the mechanism of protein-synthesis inhibition by abrin and ricin. Eur. J. Biochem. 59: 573-580.
14. Budavari S. 1989. The Merck Index: an Encyclopedia of Chemicals, Drugs, and Biologicals, 10th edn. Merck: Rahway, NJ.
15. Butler WH, Ford GP, Creasy DM. 1996. A 90-day feeding study of lupin (Lupinus angustifolius) flour spiked with lupin alkaloids in the rat. Food Chem. Toxicol. 34(6): 531-536.
16. Caligari S, Chiesa G, Johnson SK, Camisassi D, Gilio D, Marchesi M, Parolini C, Rubio LA, Sirtori CR. 2006. Lupin (Lupinus albus) protein isolate (L-ISO) has adequate nutritional value and reduces large intestinal weight in rats after restricted and ad libitum feeding. Ann. Nutr. Metab. 50(6): 528-537.
17. Carlini CR, Grossi-de-Sá MF. 2002. Plant toxic proteins with insecticidal properties. A review on their potentialities as bioinsecticides. Toxicon 40: 1515-1539.
18. Castilho PV, Goto LS, Roberts LM, Araújo APU. 2008. Isolation and characterization of four type2 ribosome inactivating pulchellin isoforms from Abruspulchellus seeds. FEBS J. 275(5): 948-959.
19. Chambery A, Di Maro A, Monti MM, Stirpe F, Parente A. 2004. Volkensin from Adenia volkensii Harms (kilyambiti plant), a type 2 ribosome-inactivating protein. Eur. J. Biochem. 271(1): 108-117.
20. Chambery A, Severino V, Stirpe F, Parente A. 2007. Cloning and expression of the B chain of volkensin, type 2 ribosome inactivating protein from Adenia volkensii harms: co-folding with the A chain for heterodimer reconstitution. Protein Expression Purif. 51(2): 209-215.
21. Chen YL, Chow LP, Tsugita A, Lin JY. 1992. The complete primary structure of abrin-a B chain. FEBS Lett. 309: 115-118.
22. Clark K. 1997. The Chemical Weapons Convention: Chemical and Toxin Warfare Agents and Plant Toxic Proteins and their Significance Disarmament. Royal Military College of Science, Cranfield University: Cranfield.
23. Cordain L, Toohey L, Smith MJ, Hickey MS. 2000. Modulation of immune function by dietary lectins in rheumatoid arthritis. Br. J. Nutr. 83: 207-217.
24. Csáky I, Fekete S. 2004. Soybean: feed quality and safety. Part 1: biologically active components: a review. Acta Vet. Hung. 52(3): 299-313; doi: 10.1556/AVet.52.2004.3.6.
25. De Benitoa FM, Iglesiasa R, Ferrerasa JM, Citoresa L, Camafeitab E, Méndezb E, Girbésa T. 1998. Constitutive and inducible type 1 ribosome-inactivating proteins (RIPs) in elderberry (Sambucus nigra L.). FEBS Lett. 428(1): 75-79.
26. Delaney B, Astwood JD, Cunny H, Eichen Coon R, Herouet-Guicheney C, MacIntosh S, Meyer LS, Privalle L, Gao Y, Mattsson J, Levine M. 2008. Evaluation of protein safety in the context of agricultural biotechnology. Food Chem. Toxicol. 46: S71-S97.
27. Dickers KJ, Bradberry SM, Rice P, Griffiths GD, Vale JA. 2003. Abrin poisoning. Toxicol. Rev. 22(3): 137-42.
28. Di Cola A, Marcozzi G, Balestrini R, Spanò L. 1999. Localization of the type 1 ribosome-inactivating protein, luffin, in adult and embryonic tissues of Luffa cylindrica L. Roem. J. Exp. Bot. 50(334): 573-579; doi: 10.1093/jxb/50.334.573.
29. Egaiia JI, Uauy R, Cassorla X, Barrera G, Yanez E. 1992. Sweet lupin protein quality in young men. J. Nutr. 122(12): 2341-2347.
30. Ellenhorn MJ, Barceloux DG. 1988. Medical Toxicology. Elsevier: New York; 1224-1225.
31. Endo Y, Tsurugi K. 1988. The RNA N-glycosidase activity of ricin A-chain: the characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. J. Biol. Chem. 263: 8735-8739.
32. Endo Y, Tsurugi K, Lambert JM. 1988. The site of action of six different ribosome-inactivating proteins from plants on eukaryotic ribosomes: the RNA N-glycosidase activity of the proteins. Biochem. Biophys. Res. Commun. 150: 1032-1036.
33. Fennema WR. 1985. Food Chemistry, 2nd edn, revised and expanded. Marcel Dekker: New York.
34. Follmer C, Barcellos GBS, Zingali RB, Machado OLT, Alves EW, Barja-Fidalgo C, Guimaran ESS, Carlini CR. 2001. Canatoxin, a toxic protein from jack beans (Canavalia ensiformis), is a variant form of urease (EC 3.5.1.5): biological effects of urease independent of its ureolytic activity. Biochem. J. 360: 217-224.
35. Frape D. 2010. Equine Nutrition and Feeding, 4th edn. Wiley-Blackwell: Chichester.
36. Gasperi-Campani A, Barbieri L, Lorenzoni E, Montanaro L, Sperti S, Bonetti E, Stirpe F. 1978. Modeccin, the toxin of Adenia digitata, purification, toxicity and inhibition of protein synthesis in vitro. Biochem. J. 174: 491-496.
37. Gattas Zaror V, Barrera Acevedo G, Yafiez Soto E, Uauy-Dagach Imbarack R. 1990. Evaluacion de la tolerancia y aceptabilidad cronica de la harina de lupino (Lupinus albus var. Multolupa) en la alimentacion de adultos jovenes. [Tolerance and chronic acceptability evaluation of lupine (Lupinus albus var. Multolupa) flour in young adults.] Archiv. Latinoam. Nutr. 40(4): 490-502.
38. Girbés T, Citores L, Iglesias R, Ferreras JM, Muñoz R, Rojo MA, Arias FJ, García JR, Méndez E, Calonge M. 1993. Ebulin 1, a nontoxic novel type 2 ribosome-inactivating protein from Sambucus ebulus L. leaves. J. Biol. Chem. 268: 18195-18199.
39. Girbés T, Ferreras JM, Arias FJ, Stirpe F. 2004. Description, distribution, activity and phylogenic relationship of ribosome-inactivating proteins in plants, fungi and bacteria. Mini Rev. Med. Chem. 4: 467-482.
40. Goldstein IJ, Poretz RD. 1986. Isolation, physicochemical characterization, and carbohydrate-binding specificity of lectins. In The Lectins Properties, Functions and Applications in Biology and Medicine, Goldstein IJ, Liener IE, Sharon N (eds). Academic: San Diego, CA;233-247.
41. Grant G, Dorward PM, Pusztai A. 1993. Pancreatic enlargement is evident in rats fed diets containing raw soybeans (Glycine max) or cowpeas (Vigna unguiculata) for 800days but not in those fed diets based on kidney beans (Phaseolus vulgaris) or lupinseed (Lupinus angustifolius). J. Nutr. 123(12): 2207-2215.
42. Grant G, Dorward PM, Buchan WC, Armour JC, Pustzai A. 1995. Consumption of diets containing raw soya beans (Glycine max), kidney beans (Phaseolus vulgaris), cowpeas (Vigna unguiculata) or lupin seeds (Lupinus angustifolius) by rats for up to 700days: effects on body composition and organ weights. Br. J. Nutr. 73(1): 17-29.
43. Gunsolus JM. 1955. Toxicity of Jequirity beans. JAMA 157: 779.
44. Hall RS, Johnson SK. 2004. Sensory acceptability of foods containing Australian sweet lupin (Lupinus angustifolius) flour. J. Food Sci. 69(2): SNQ92-SNQ97.
45. Hall RS, Thomas SJ, Johnson SK. 2005. Australian sweet lupin flour addition reduces the glycaemic index of a white bread breakfast without affecting palatability in healthy human volunteers. Asia Pacific J. Clin. Nutr. 14(1): 91-97.
46. Hammond B, Cockburn A. 2008. The safety assessment of proteins introduced into crops developed through agricultural bio-technology: a consolidated approach to meet current and future needs. In Food Safety of Proteins in Agricultural Biotechnology, Hammond BG (ed.). CRC Press, Taylor and Francis: New York; 259-288.
47. Hammond BG, Jez JM. 2011. Impact of food processing on the safety assessment for proteins introduced into biotechnology-derived soybean and corn crops. Food Chem. Toxicol. 49(4): 711-721.
48. Hellin H. 1891. Der Eiwesskorpe Abrin; Sieve Wirkung auf Blut., Thesis, University of Dorpat, Dorpat (Tartu).
49. Honavar PM, Shih CV, Liener IE. 1962. The inhibition of growth of rats by purified hemagglutinin fractions isolated from Phaseolus vulgaris. J. Nutr. 77: 109-114.
50. Hudak KA, Wang P, Tumer NE. 2000. A novel mechanism for inhibition of translation by pokeweed antiviral protein: depurination of the capped RNA template. RNA 6: 369-380.
51. Jaffé WG. 1960. Uber Phytotoxine und Bohnen. Arzneimittel-Forsch./Drug Res. 10: 1012-1016.
52. Janzen DH, Ryan CA, Liener IE, Pearce G. 1986. Potentially defensive proteins in mature seeds of 59 species of tropical leguminosae. J. Chem. Ecol. 12(6): 1469-1480.
53. Joshi AL. 1972. Studies in proteins of double bean (P. lunatus) with special reference to its hemagglutinins. Toxicon 10: 89-91.
54. Katzin BJ, Collins EJ, Robertus JD. 1991. Structure of ricin A-chain at 2.5Å. Proteins 10(3): 251-259.
55. Kimura M, Sumizawa T, Funatsu G. 1993. The complete amino acid sequences of the B-chains of abrin-a and abrin-b, toxic proteins from the seeds of Abrus precatorius. Biosci. Biotechnol. Biochem. 57: 166-169.
56. Krauspenhaar R, Eschenburg S, Perbandt M, Kornilov V, Konareva N, Mikailova I, Stoeva S, Wacker R, Maier T, Singh T, Mikhailov A, Voelter W, Betzel C. 1999. Crystal structure of mistletoe lectin I from Viscum album. Biochem. Biophys. Res. Commun. 257: 418-424.
57. Kruger CL, Marano KM, Morita Y, Takada Y, Kawakami H, Kobayashi T, Sunaga M, Furukawa M, Kawamura K. 2007. Safety evaluation of a milk basic protein fraction. Food Chem. Toxicol. 45(7): 1301-1307.
58. Kunitz M. 1945. Crystallization of a trypsin inhibitor from soybeans. Science 101: 668-669.
59. Lee YP, Mori TA, Sipsas S, Barden A, Puddey IB, Burke V, Hall RS, Hodgson JM. 2006. Lupin-enriched bread increases satiety and reduces energy intake acutely. Am. J. Clin. Nutr. 84(5): 975-980. [Erratum 85(4), 1166.].
60. Li MX, Yeung HW, Pan LP, Chan SI. 1991. Trichosanthin, a potent HIV-1 inhibitor, can cleave supercoiled DNA in vitro. Nucl. Acids Res. 19: 6309-6312.
61. Liener E, Pallansch MJ. 1952. Purification of a toxic substance from de-fatted soy bean flour. J. Biol. Chem. 197: 29-36.
62. Liener IE, Rose JE. 1953. Soyin, a toxic protein from the soybean III. Im-munochemical properties. Proc. Soc. Exp. Biol. Med. 83: 539-544.
63. Lin JY, Tserng KY, Chen CC, Lin LT, Tung TC. 1970. Abrin and ricin: new anti-tumour substances. Nature 227: 292 - 293; doi: 10.1038/227292a0.
64. Lin J, Yan F, Tang L, Chen F. 2002. Isolation, purification and functional investigation on the N-glycosidase activity of curcin from the seeds of Jatropha curcas. High Technol. Lett. 11: 36-40.
65. Loew FM, Doige CE, Manns JG, Searcy GP, Bell JM, Jones JD. 1976. Evaluation of dietary rapeseed protein concentrate flours in rats and dogs. Toxicol. Appl. Pharmacol. 35(2): 257-267.
66. Lord JM, Roberts LM, Robertus JD. 1994. Ricin: structure, mode of action, and some current applications. FASEB J. 8: 201-208.
67. Loris R, Hamelryck T, Bouckaert J, Wyns L. 1998. Legume lectin structure. Biochim. Biophys. Acta 1383(1): 9-36; doi: 10.1016/S0167-4838(97)00182-9.
68. Magni C, Sessa F, Accardo E, Vanoni M, Morazzoni P, Scarafoni A, Duranti M. 2004. Conglutin γ, a lupin seed protein, binds insulin in vitro and reduces plasma glucose levels of hyperglycemic rats. J. Nutr. Biochem. 15(11): 646-650.
69. Mejia LA, Korgaonkar CK, Schweizer M, Chengelis C, Marit G, Ziemer E, Grabiel R, Empie M. 2009a. A 13-week sub-chronic dietary toxicity study of a cruciferin-rich canola protein isolate in rats. Food Chem. Toxicol. 47(10): 2645-2654.
70. Mejia LA, Korgaonkar CK, Schweizer M, Chengelis C, Novilla M, Ziemer E, Williamson-Hughes PS, Grabiel R, Empie M. 2009b. A 13-week dietary toxicity study in rats of a napin-rich canola protein isolate. Regulat. Toxicol. Pharmacol. 55(3): 394-402.
71. Min W, Dunn AJ, Jones DH. 1992. Non-glycosylated recombinant pro-concanavalin A is active without polypeptide cleavage. EMBO J. 11(4): 1303-7.
72. Miyake K, Tanaka T, McNeil PL. 2007. Lectin-based food poisoning: a new mechanism of protein toxicity. PLoS One 2(1): e687; doi: 10.1371/journal.pone.0000687.PMC1933252.
73. Moisenovich M, Tonevitsky A, Agapov I, Niwa H, Schewe H, Bereiter-Hahn J. 2002. Differences in endocytosis and intracellular sorting of ricin and viscumin in 3T3 cells. Eur. J. Cell Biol. 81(10): 529-538.
74. Montfort W, Villafranca JE, Monzingo AF, Ernst SR, Katzin B, Rutenber E, Xuong NH, Hamlin R, Robertus JD. 1987. The three-dimensional structure of ricin at 2.8Å. J. Biol. Chem. 262: 5398-5403.
75. Morris KN, Wool IG. 1994. Analysis of the contribution of an amphiphilic alpha-helix to the structure and to the function of ricin A chain. Proc. Natl Acad. Sci. USA 91: 7530-7533.
76. Myers BA, Hathcock J, Shiekh N, Roebuck BD. 1991. Effects of dietary soya bean trypsin inhibitor concentrate on initiation and growth of putative preneoplastic lesions in the pancreas of the rat. Food Chem. Toxicol. 29(7): 437-443.
77. Olsnes S, Kozlov JV. 2001. Ricin. Toxicon 39: 1723-1728.
78. Olsnes S, Pihl A. 1976. Kinetics of binding of the toxic lectins abrin and ricin to surface receptors of human cells. J. Biol. Chem. 251: 3977-3984.
79. Olsnes S, Sandvig K, Eiklid K, Pihl A. 1978. Properties and action mechanism of the toxic lectin modeccin: interaction with cell lines resistant to modeccin, abrin, and ricin. J. Supramol. Struct. 9: 15-25.
80. Olsnes S, Stirpe F, Sandvig K, Pihl A. 1982. Isolation and characterization of viscumin, a toxic lectin from Viscum album L. (mistletoe). J. Biol. Chem. 257(22): 13263-13270.
81. Osborne TB, Mendel LB. 1917. The use of soybean as food. J. Biol. Chem. 32: 369-387.
82. Parka JH, Hyunb CK, Shinb HK. 1998. Cytotoxicity of heat-treated Korean mistletoe. Cancer Lett. 126(1): 43-48.
83. Patočka J, Středa L. 2003. Plant toxic proteins and their current significance for warfare and medicine. J. Appl. Biomed. 1:141-147.
84. Plass R, Bleyl DWR, Lewerenz HJ, Kroll J. 2006. Toxicological evaluation of rapeseed products in a sub-acute feeding study in rats. Food Nahrung 36(3): 248-252, 1992.
85. Puri M, Kaur I, Kanwar RK, Gupta RC, Chauhan A, Kanwar JR. 2009. Ribosome Inactivating Proteins (RIPs) from Momordica charantia for Anti Viral Therapy. Curr. Mol. Med. 9: 1080-1094.
86. Pusztai A, Grant G, Gelencser E, Ewen SWB, Pfuller U, Eifler R, Bardocz S. 1998. Effects of an orally administered mistletoe (type-2 RIP) lectin on growth, body composition, small intestinal structure, and insulin levels in young rats. J. Nutr. Biochem. 9: 31-36.
87. Puttaraj S, Bhagya S, Murthy KN, Singh N. 1994. Effect of detoxification of castor seed (Ricinus communis) protein isolate on its nutritional quality. Plant Foods Hum. Nutr. (formerly Qualitas Plantarum) 46(1): 63-70; doi: 10.1007/BF01088462.
88. Rackis JJ, Gumbmann MR. 1981. Protease inhibitors: physiological properties and nutritional significance. In Antinutrients and Natural Toxicants in Foods, Ory RL (ed.). Food and Nutrition Press: Westport, CT; 203-237.
89. Rahman MH. 2000. The nutritional toxicity of sweet lupin (Lupinus angustifolius) seed proteins. J. Sci. Food Agric. 80(1): 72-78.
90. Rahman MH, Hossain A, Siddiqua A, Hossain I. 1996. Hemato-biochemical parameters in rats fed Lupinus angustifolius L. (sweet lupin) seed protein and fibre fractions. J. Clin. Biochem. Nutr. 20(2): 99-111.
91. Refsnes K, Haylett T, Sandvig K, Olsnes S. 1977. Modeccin - a plant toxin inhibiting protein synthesis. Biochem. Biophys. Res. Commun. 79: 1176-1183.
92. Rutenber E, Robertus JD. 1991. Structure of ricin B-chain at 2.5Å resolution. Proteins 10: 260-269.
93. Ryan CA, Haas GM. 1981. Structural, evolutionary and nutritional properties of protease inhibitors from potatoes. In Antinutrients and Natural Toxicants in Foods, Ory RL (ed.). Food and Nutrition Press: Westport, CT; 169-185.
94. Sandvig K, Olsnes S, Pihl A. 1978. Chemical modifications of the toxic lectins abrin and ricin. Eur. J. Biochem. 84: 323-331.
95. Sandvig K, Torgersen ML, Engedal N, Skotland T, Iversen TG. 2010. Protein toxins from plants and bacteria: probes for intracellular transport and tools in medicine. FEBS Lett. 584(12): 2626-2634.
96. Schaafsma G. 2009. Safety of protein hydrolysates, fractions thereof and bioactive peptides in human nutrition. Eur. J. Cli. Nutr. 63: 1161-1168; doi: 10.1038/ejcn.
97. Scientific Opinion of the Panel on Contaminants in the Food Chain, European Food Safety Authority. 2008. Ricin (from Ricinus communis) as undesirable substances in animal feed. EFSA J. 726: 1-38.
98. Sharon N, Lis H. 2004. History of lectins: from hemagglutinins to biological recognition molecules. Glycobiology 14(11): 53R-62R; doi: 10.1093/glycob/cwh122.
99. Sharp PE, LaRegina MC. 1998. Important biological features. In The Laboratory Rat. Laboratory Animal Pocket Reference Series. CRC Press: Boca Raton, FL; 1-19.
100. Shih RD, Goldfrank LR. 1998. Plants. In Goldfrank's Toxicologic Emergencies 6, Goldfrank LR, Flomenbaum NE, Lewin NA, Weisman RS, Howland MA, Hoffman RS (eds). Appleton and Lange: East Norwalk, CT.
101. Silva ALC, Goto LS, Dinarte AR, Hansen D, Moreira RA, Beltramini LM, Araújo APU. 2005. Pulchellin, a highly toxic type 2 ribosome-inactivatingprotein from Abrus pulchellus Cloning, heterologous expression of A-chain and structural studies. FEBS J. 272: 1201-1210.
102. Sirtori CR, Lovati MR, Manzoni C, Castiglioni S, Duranti M, Magni C, Morandi S, D'Agostina A, Arnoldi A. 2004. Proteins of white lupin seed, a naturally isoflavone-poor legume, reduce cholesterolemia in rats and increase LDL receptor activity in HepG2 cells. J. Nutr. 134(1): 18-23.
103. Stillmark H. 1888. Ueber Ricin, ein giftiges Ferment aus dem Samen von Ricinus communis L. und einigen anderen Euphorbiaceen. Arb. Pharmak. Inst. Dorpat 3: 59-151.
104. Stirpe F. 2004. Ribosome-inactivating proteins. Toxicology 44: 371-383.
105. Stirpe F, Battelli MG. 2006. Risobosome-inactivating proteins: progress and problems. Cell. Mol. Life Sci. 63: 1850-1866.
106. Stirpe F, Pession-Brizzi A, Lorenzoni E, Strocchi P, Montanaro L, Sperti S. 1976. Studies on the proteins from the seeds of Croton tiglium and of Jatropha curcas. Biochem. J. 156: 1-6.
107. Stirpe F, Barbieri L, Abbondanza A, Falasca AI, Brown AN, Sandvig K, Olsnes S, Pihl A. 1985. Properties of volkensin, a toxic lectin from Adenia volkensii. J. Biol. Chem. 260: 14589-14595.
108. Stirpe F, Barbieri L, Battelli MG, Soria M, Lappi DA. 1992. Ribosome inactivating proteins from plants: present status and future prospects. Bio/Technology 10: 405-412.
109. Stirpe F, Barbieri L, Gorini P, Valbonesi P, Bolognesi A, Polito L. 1996. Activities associated with the presence of ribosome-inactivating proteins increase in senescent and stressed leaves. FEBS Lett. 382: 309-312.
110. Stirpe F, Bolognesi A, Bortolotti M, Farini V, Lubelli C, Pelosi E, Polito L, Dozza B, Strocchi P, Chambery A, Parente A, Barbieri L. 2007. Characterization of highly toxic type 2 ribosome-inactivating proteins from Adenia lanceolata and Adenia stenodactyla (Passifloraceae). Toxicon 50(1): 94-105.
111. Stobiecki M, Blaszczyk B, Kowalczyk-Bronisz SH, Gulewicz K. 1993. The toxicity of seed extracts and their fractions from Lupinus agnustifolius L. and Lupinus albus L. J. Appl. Toxicol. 13(5): 347-352.
112. Sumner JB, Gralën N, Eriksson-Quensel IB. 1938. The molecular weights of canavalin, concanavalin A, and Concanavalin B. J. Biol. Chem. 125(2261): 45-48; doi: 10.1126/science.87.2261.395.
113. Tobiska J. 1964. Die Phyth1imagglutinine. Akademie: Berlin.
114. Tripathi S, Maity TK. 2003. Stimulation of murine macrophages by native and heat-denatured lectin from Abrus precatorius. Int. Immunopharmacol. Immunotoxicol. 3: 375-381.
115. Tripathi S, Ghosh D, Maity TK. 2004. Immunostimulatory role of tryptic digest of Abrus precatorius agglutinin. Int. Immunopharmacol. Immunotoxicol. 26: 411-424.
116. Van Damme EJM, Peumans WJ, Pusztai A, Bardocz B. 1998. Handbook of Plant Lectins: Properties and Biomedical Applications. Wiley: Chichester; 417-421.
117. Vasconcelos IM, Trentim A, Guimarães JA, Carlini CR. 1994. Purification and physicochemical characterization of soyatoxin, a novel toxicprotein isolated from soybeans(Glycine max). Arch. Biochem. Biophys. 312(2): 357-366.
118. Vivanco JM, Savary BJ, Flores HE. 1999. Characterization of two novel type I ribosome-inactivating proteins from the storage roots of the Andean crop Mirabilis expansa. Plant Physiol. 119(4): 1447-1456.
119. Weijers HA, van de Kamer JH. 1965. Some considerations of celiac disease. Am. J. Clin. Nutr. 17: 51-54.
120. Wu W, Sun Y. 2011. Dietary safety evaluation of water hyacinth leaf protein concentrate. Hum. Exp. Toxicol. 30: 1514-1520; doi: 10.1177/0960327110392085.
121. Wu W, Yang X. 2011. Decontamination of aquatic vegetable leaves by removing trace toxic metals during pickling process with acetic acid solution. Ecol. Food Nutr. 50: 368-374.