Vicine is hydrolyzed by microflora to highly reactive free radical generating compound divicine which causes mortality and other adverse effects. This study in the rats established the effect of a broad spectrum and poorly absorbed antibiotic, neomycin sulfate on the toxicity of vicine. The results showed extremely decrease in mortality rate in the group pretreated with neomycin. Hemoglobin (Hb) concentration, hematocrit (Hct) value, and red blood cells (RBCs) count were significantly decreased after injection of vicine and the improvement of these values in the group pretreated with neomycin. The same results were observed in white blood cells (WBCs). The results showed a significant decrease in glucose level and returned to normal in group pretreated with neomycin. Glutathione (GSH) was significantly decreased in the vicine group and returned to normal value in the group pretreated with neomycin. Lipid peroxide (TBARs) was significantly increased in the group treated with vicine and neomycin pretreated group decreased to the normal level. Glucose-6-phosphate dehydrogenase (G6-PD) activity was significantly decreased and returned to normal level in rats pretreated with neomycin. Serum protein and globulin were significantly decreased but serum albumin showed insignificant decrease in vicine and neomycin groups compared to control. Alanine aminotransferase (ALT) and aspartate aminotransferase (AST) were significantly decreased in the vicine group. The group pretreated with neomycin showed significantly increased activities of AST and ALT compared with vicine group. In conclusion, neomycin pretreatment of rats injected with glycoside vicine decreased to a great extent of its toxic and mortality effects and is useful in favism and hemolytic anemia. 1. Introduction The importance of legumes in agriculture, human consumption, and animal nutrition is increasing exponentially due to the increasing world population and its need for proteins. Food legumes are considered the best substitute for meat in many parts of the world, where there is a demand for alternate, nonanimal protein sources. Legume crops have two distinctive traits: (1) their high protein content, and (2) their unique symbiotic ability to fix atmospheric nitrogen in the soil. Faba bean (Vicia faba L.) is an important member of the legume family with highly useful characteristics. The world production of faba beans is close to 4.5 millions of tons. Faba bean is the second most important legume crop in Europe, which accounts for 14% of the world area and about 25% of the world production [1]. It
G. Duc, P. Marget, R. Esnault, J. le Guen, and D. Bastianelli, “Genetic variability for feeding value of faba bean seeds (Vicia faba): comparative chemical composition of isogenics involving zero-tannin and zero-vicine genes,” Journal of Agricultural Science, vol. 133, no. 2, pp. 185–196, 1999.
[3]
R. Randhir and K. Shetty, “Microwave-induced stimulation of L-DOPA, phenolics and antioxidant activity in fava bean (Vicia faba) for Parkinson's diet,” Process Biochemistry, vol. 39, no. 11, pp. 1775–1784, 2004.
[4]
Z. Madar and A. H. Stark, “New legume sources as therapeutic agents,” British Journal of Nutrition, vol. 88, no. 3, pp. S287–S292, 2002.
[5]
H. Ray and F. Georges, “A genomic approach to nutritional, pharmacological and genetic issues of faba bean (Vicia faba): prospects for genetic modifications,” GM Crops, vol. 1, no. 2, pp. 99–106, 2010.
[6]
Z. Bicakci, “A hemolysis trigger in glucose-6-phosphate dehydrogenase enzyme deficiency. Vicia sativa (Vetch),” Saudi Medical Journal, vol. 30, no. 2, pp. 292–294, 2009.
[7]
N. Gutierrez, C. M. Avila, G. Duc et al., “CAPs markers to assist selection for low vicine and convicine contents in faba bean (Vicia faba L.),” Theoretical and Applied Genetics, vol. 114, no. 1, pp. 59–66, 2006.
[8]
G. Hawatin and R. Stewart, “The development, production and problems of faba bean (Vicia faba L.) in West Asia and North Africa,” Fabis Newsletter, vol. 1, pp. 7–9, 1979.
[9]
M. I. Hegazy and R. R. Marquardt, “Metabolism of vicine and convicine in rat tissues: absorption and excretion patterns and sites of hydrolysis,” Journal of the Science of Food and Agriculture, vol. 35, no. 2, pp. 139–146, 1984.
[10]
J. Y. Lin and K. H. Ling, “Studies on favism. I. Isolation of an active principle from faba beans (Vicia faba),” Journal of the Formosan Medical Association, vol. 61, pp. 484–489, 1962.
[11]
M. S. Arbid and R. R. Marquardt, “Effect of intraperitoneally injected vicine and convicine on the rats: induction of favism-like sign,” Journal of the Science of Food and Agriculture, vol. 37, no. 6, pp. 539–547, 1986.
[12]
M. D'Aquino, S. Gaetani, and M. A. Spadoni, “Effect of factors of favism on the protein and lipid components of rat erythrocyte membrane,” Biochimica et Biophysica Acta, vol. 731, no. 2, pp. 161–167, 1983.
[13]
R. R. Marquardt, D. S. Muduuli, and A. A. Frohlish, “Purification and some properties of vicine and convicine isolated from faba beans (Vicia faba L) protein concentrate,” Journal of Agriculture and Food Science, vol. 31, pp. 839–844, 1983.
[14]
M. Vilari？o, J. P. Métayer, K. Crépon, and G. Duc, “Effects of varying vicine, convicine and tannin contents of faba bean seeds (Vicia faba L.) on nutritional values for broiler chicken,” Animal Feed Science and Technology, vol. 150, no. 1-2, pp. 114–121, 2009.
[15]
M. T. Farran, A. H. Darwish, M. G. Uwayjan, F. T. Sleiman, and V. M. Ashkarian, “Vicine and convicine in common vetch (Vicia sativa) seeds enhance β-cyanoalanine toxicity in male broiler chicks,” International Journal of Toxicology, vol. 21, no. 3, pp. 201–209, 2002.
[16]
P. Cuevas, F. Carceller, D. Diaz-González et al., “Inhibition of rat glioma growth by neomycin. Preliminary report,” Neurological Research, vol. 24, no. 6, pp. 522–524, 2002.
[17]
M. G. Turtay, C. Firat, E. Samdanci, H. Oguzturk, S. Erbatur, and C. Colak, “Effects of montelukast on burn wound healing in a rat model,” Clinical and Investigative Medicine, vol. 33, no. 6, pp. E413–E421, 2010.
[18]
X. Sun, V. Kishore, K. Fites, and O. Akkus, “Osteoblasts detect pericellular calcium concentration increase via neomycin-sensitive voltage gated calcium channels,” Bone, vol. 51, pp. 860–867, 2012.
[19]
N. Szentmáry, S. Goebels, P. Matoula, F. Schirra, and B. Seitz, “Acanthamoeba keratitis-a rare and often late diagnosed disease,” Klinische Monatsbl？tter für Augenheilkunde, vol. 229, no. 5, pp. 521–528, 2012.
[20]
L. Wang, A. Pulk, M. R. Wasserman et al., “Allosteric control of the ribosome by small-molecule antibiotics,” Nature Structural & Molecular Biology, vol. 19, no. 9, pp. 957–963, 2012.
[21]
R. R. Marquardt, D. S. Muduuli, and A. A. Frohlich, “Purification and some properties of vicine and convicine isolated from faba bean (Vicia faba L.) protein concentrate,” Journal of Agricultural and Food Chemistry, vol. 31, no. 4, pp. 839–844, 1983.
[22]
L. C. Rodak, “Routing testing in haematology,” in Dignostic Haematology, pp. 128–144, W.B. Saunders, Philadelphia, Pa, USA, 1995.
[23]
E. J. van Kampen and W. G. Zijlstra, “Standardization of hemoglobinometry II. The hemiglobincyanide method,” Clinica Chimica Acta, vol. 6, no. 4, pp. 538–544, 1961.
[24]
E. Beutler, O. Duron, and B. M. Kelly, “Improved method for the determination of blood glutathione,” The Journal of Laboratory and Clinical Medicine, vol. 61, pp. 882–888, 1963.
[25]
R. J. Henry, Clinical Chemistry Principle and Techniques, Harper and Row, New York, NY, USA, 1968.
[26]
S. Reitman and S. Frankel, “A colorimetric method for the determination of serum glutamic oxalacetic and glutamic pyruvic transaminases,” American Journal of Clinical Pathology, vol. 28, no. 1, pp. 56–63, 1957.
[27]
P. Trinder, “Determination of glucose in blood using glucoseoxidase with an alternative oxygen acceptor,” Annals Clinical Biochemistry, vol. 6, pp. 24–27, 1969.
[28]
T. Yoshioka, K. Kawada, T. Shimada, and M. Mori, “Lipid peroxidation in maternal and cord blood and protective mechanism against activated-oxygen toxicity in the blood,” American Journal of Obstetrics and Gynecology, vol. 135, no. 3, pp. 372–376, 1979.
[29]
G. W. Loher and H. D. Waller, “Glucose-6- phosphate dehydrogenase,” in Method of Enzymatic Analysis, H. U. Bergmeyer, Ed., pp. 636–649, Academic Press, New York, NY, USA, 1974.
[30]
A. A. Frohlich and R. R. Marquardt, “Turnover and hydrolysis of vicine and convicine in avian tissues and digesta,” Journal of the Science of Food and Agriculture, vol. 34, no. 2, pp. 153–163, 1983.
[31]
M. A. Belsey, “The epidemiology of favism,” Bulletin of the World Health Organization, vol. 48, no. 1, pp. 1–13, 1973.
[32]
L. S. Goodman and A. Gilman, The Pharmacological Basis of Therapeutics, Macmillan Publishing, New York, NY, USA, 5th edition, 1975.
[33]
M. S. S. Arbid, M. S. Madhyastha, R. R. Marquardt, and A. A. Frohlich, “Effect of neomycin on the hydrolysis and toxicity of vicine and convicine in rats,” Food and Chemical Toxicology, vol. 31, no. 11, pp. 835–840, 1993.
[34]
M. S. S. Arbid and R. R. Marquardt, “Favism-like effects of divicine and isouramil in the rat: acute and chronic effects on animal health, mortalities, blood parameters and ability to exchange respiratory gases,” Journal of the Science of Food and Agriculture, vol. 43, no. 1, pp. 75–90, 1988.
[35]
D. C. McMillan and D. J. Jollow, “Favism: divicine hemotoxicity in the rat,” Toxicological Sciences, vol. 51, no. 2, pp. 310–316, 1999.
[36]
S. Yannai and R. R. Marquardt, “Induction of favism-like symptoms in the rat: effects of vicine and divicine in normal and buthionine sulfoximine-treated rats,” Journal of the Science of Food and Agriculture, vol. 36, no. 11, pp. 1161–1168, 1985.
[37]
J. J. Kaneko, Clinical Biochemistry of Domestic Animals, Academic Press, New York, NY, USA, 3rd edition, 1980.
[38]
M. Comporti, “Lipid peroxidation and cellular damage in toxic liver injury,” Laboratory Investigation, vol. 53, no. 6, pp. 599–623, 1985.
[39]
M. M. Abbady, Biochemical changes in irradiated animals exposed to some environmental pollutants [Ph.D. thesis], Faculty of Science, Ain Shams University, Cairo, Egypt, 1994.
[40]
V. Perman, “Synovial fluid,” in Clinical Biochemistry of Domestic Animals, J. Kaneko, Ed., pp. 68–93, Academic Press, New York, NY, USA, 3rd edition, 1980.
[41]
R. R. Marquardt, N. Wang, and M. S. S. Arbid, “Pyrimidine glycosides,” in Handbook of Plant and Fungal Toxicants, J. O. F. D'Mello, Ed., chapter 10, pp. 139–155, CRC Press, Boca Raton, Fla, USA, 1997.
[42]
E. Beutler, “Hemolytic anemia in disorders of red cell metabolism,” in Topics in Hematology, M. M. Wintrobe, Ed., pp. 199–209, Plenum Publishing, New York, NY, USA, 1978.
[43]
M. Zhang, G. Song, and G. Y. Minuk, “Effects of hepatic stimulator substance, herbal medicine, selenium/vitamin E, and ciprofloxacin on cirrhosis in the rat,” Gastroenterology, vol. 110, no. 4, pp. 1150–1155, 1996.
