메뉴 건너뛰기




Volumn 157, Issue 1-2, 2010, Pages 41-54

In vitro ruminal degradation of ricin and its effect on microbial growth

Author keywords

Castorseed; Detoxification; Electrophoresis; Toxin

Indexed keywords

BOVIDAE; RICINUS COMMUNIS;

EID: 77949914988     PISSN: 03778401     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.anifeedsci.2010.01.006     Document Type: Article
Times cited : (23)

References (43)
  • 1
    • 77949917485 scopus 로고
    • Castor meal for growing-finishing steers
    • (Abstr)
    • Albin R.C., Davis W.H., and Zinn D.W. Castor meal for growing-finishing steers. J. Anim. Sci. 28 Suppl. 1 (1969) 133 (Abstr)
    • (1969) J. Anim. Sci. , vol.28 , Issue.SUPPL. 1 , pp. 133
    • Albin, R.C.1    Davis, W.H.2    Zinn, D.W.3
  • 2
    • 0030336463 scopus 로고    scopus 로고
    • Experimental poisoning of sheep with seeds of Ricinus communis
    • (in Portuguese, with English abstract)
    • Armién A.G., D'Angelis F.H.F., and Tokarnia C.H. Experimental poisoning of sheep with seeds of Ricinus communis. Pesq. Vet. Bras. 16 (1996) 99-106 (in Portuguese, with English abstract)
    • (1996) Pesq. Vet. Bras. , vol.16 , pp. 99-106
    • Armién, A.G.1    D'Angelis, F.H.F.2    Tokarnia, C.H.3
  • 4
    • 27744564219 scopus 로고    scopus 로고
    • Ricin poisoning: a comprehensive review
    • Audi J., Belson M., Patel M., Schier J., and Osterloh J. Ricin poisoning: a comprehensive review. JAMA 294 (2005) 2342-2351
    • (2005) JAMA , vol.294 , pp. 2342-2351
    • Audi, J.1    Belson, M.2    Patel, M.3    Schier, J.4    Osterloh, J.5
  • 5
    • 0017184389 scopus 로고
    • A rapid sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M.M. A rapid sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 33646400526 scopus 로고
    • Modified reagents for determination of urea and ammonia
    • Chaney A.L., and Marbach E.P. Modified reagents for determination of urea and ammonia. Clin. Chem. 8 (1962) 130-132
    • (1962) Clin. Chem. , vol.8 , pp. 130-132
    • Chaney, A.L.1    Marbach, E.P.2
  • 8
    • 0024659698 scopus 로고
    • More monensin-sensitive, ammonia-producing bacteria from the rumen
    • Chen G., and Russell J.B. More monensin-sensitive, ammonia-producing bacteria from the rumen. Appl. Environ. Microbiol. 55 (1989) 1052-1057
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 1052-1057
    • Chen, G.1    Russell, J.B.2
  • 9
    • 0344196948 scopus 로고    scopus 로고
    • Protein sub-fractions and amino acid profiles of rumen-undegradable protein in dairy cows from soybean, cottonseed and fish meals
    • Chiou P.W.S., and Wu B.Y.S.S. Protein sub-fractions and amino acid profiles of rumen-undegradable protein in dairy cows from soybean, cottonseed and fish meals. Anim. Feed Sci. Technol. 78 (1999) 65-80
    • (1999) Anim. Feed Sci. Technol. , vol.78 , pp. 65-80
    • Chiou, P.W.S.1    Wu, B.Y.S.S.2
  • 10
    • 0019206225 scopus 로고
    • Isolation and properties of two toxic tryptic peptides from ricin, the toxin of Ricinus communis L. (castor bean) seeds
    • Creppy E.E., Lugnier A.A.J., and Dirheimer G. Isolation and properties of two toxic tryptic peptides from ricin, the toxin of Ricinus communis L. (castor bean) seeds. Toxicon 18 (1980) 649-660
    • (1980) Toxicon , vol.18 , pp. 649-660
    • Creppy, E.E.1    Lugnier, A.A.J.2    Dirheimer, G.3
  • 11
    • 0023664263 scopus 로고
    • The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28S ribosomal RNA caused by the toxins
    • Endo Y., Mitsui K., Motizuki M., and Tsurugi K. The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28S ribosomal RNA caused by the toxins. J. Biol. Chem. 262 (1987) 5908-5912
    • (1987) J. Biol. Chem. , vol.262 , pp. 5908-5912
    • Endo, Y.1    Mitsui, K.2    Motizuki, M.3    Tsurugi, K.4
  • 12
    • 0023219950 scopus 로고
    • RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes
    • Endo Y., and Tsurugi K. RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes. J. Biol. Chem. 262 (1987) 8128-8130
    • (1987) J. Biol. Chem. , vol.262 , pp. 8128-8130
    • Endo, Y.1    Tsurugi, K.2
  • 13
    • 0023947126 scopus 로고
    • The RNA N-glycosidase activity of ricin A-chain
    • Endo Y., and Tsurugi K. The RNA N-glycosidase activity of ricin A-chain. J. Biol. Chem. 263 (1988) 8735-8739
    • (1988) J. Biol. Chem. , vol.263 , pp. 8735-8739
    • Endo, Y.1    Tsurugi, K.2
  • 14
    • 0019295471 scopus 로고
    • Inhibition of Escherichia coli protein synthesis by a limited tryptic digest of ricin, the toxin of Ricinus communis L. seeds
    • Haas-Kohn L.J.G., Lugnier A.A.J., Tiboni O., Ciferri O., and Dirheimer G. Inhibition of Escherichia coli protein synthesis by a limited tryptic digest of ricin, the toxin of Ricinus communis L. seeds. Biochem. Biophys. Res. Commun. 97 (1980) 962-967
    • (1980) Biochem. Biophys. Res. Commun. , vol.97 , pp. 962-967
    • Haas-Kohn, L.J.G.1    Lugnier, A.A.J.2    Tiboni, O.3    Ciferri, O.4    Dirheimer, G.5
  • 15
    • 0037357016 scopus 로고    scopus 로고
    • Oxidative stress associated hepatic and renal toxicity induced by ricin in mice
    • Kumar O., Sugendran K., and Vijayaraghavan R. Oxidative stress associated hepatic and renal toxicity induced by ricin in mice. Toxicon 41 (2003) 333-338
    • (2003) Toxicon , vol.41 , pp. 333-338
    • Kumar, O.1    Sugendran, K.2    Vijayaraghavan, R.3
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0037164109 scopus 로고    scopus 로고
    • Nutritional significance of lectins and enzyme inhibitors from legumes
    • Lajolo F.M., and Genovese M.F. Nutritional significance of lectins and enzyme inhibitors from legumes. J. Agric. Food Chem. 50 (2002) 6592-6598
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 6592-6598
    • Lajolo, F.M.1    Genovese, M.F.2
  • 18
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H., and Burk D. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56 (1934) 658-666
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 19
    • 0017044934 scopus 로고
    • Isolation and biochemical properties of toxic tryptic peptides of ricinotoxin from Ricinus communis seeds
    • Lugnier A.A.J., Le Meur M.A., Gerlinder P., and Dirheimer G. Isolation and biochemical properties of toxic tryptic peptides of ricinotoxin from Ricinus communis seeds. Eur. J. Toxicol. Environ. Hyg. 9 (1976) 323-333
    • (1976) Eur. J. Toxicol. Environ. Hyg. , vol.9 , pp. 323-333
    • Lugnier, A.A.J.1    Le Meur, M.A.2    Gerlinder, P.3    Dirheimer, G.4
  • 20
    • 34248642605 scopus 로고    scopus 로고
    • Differential proteomic analysis of the endoplasmic reticulum from developing and germinating seeds of castor (Ricinus communis) identifies seed protein precursors as significant components of the endoplasmic reticulum
    • Maltman D.J., Gadd S.M., and Slabas A.R. Differential proteomic analysis of the endoplasmic reticulum from developing and germinating seeds of castor (Ricinus communis) identifies seed protein precursors as significant components of the endoplasmic reticulum. Proteomics 7 (2007) 1513-1528
    • (2007) Proteomics , vol.7 , pp. 1513-1528
    • Maltman, D.J.1    Gadd, S.M.2    Slabas, A.R.3
  • 21
    • 0036120467 scopus 로고    scopus 로고
    • Proteomic analysis of the endoplasmic reticulum from developing and germinating seed of castor (Ricinus communis)
    • Maltman D.J., Simon W.J., Wheeler C.H., Dunn M.J., Wait R., and Slabas A.R. Proteomic analysis of the endoplasmic reticulum from developing and germinating seed of castor (Ricinus communis). Electrophoresis 23 (2002) 626-639
    • (2002) Electrophoresis , vol.23 , pp. 626-639
    • Maltman, D.J.1    Simon, W.J.2    Wheeler, C.H.3    Dunn, M.J.4    Wait, R.5    Slabas, A.R.6
  • 22
    • 0001900904 scopus 로고
    • Use of electrophoresis to quantify ruminal degradability of protein from concentrate feeds
    • Messman M.A., and Weiss W.P. Use of electrophoresis to quantify ruminal degradability of protein from concentrate feeds. Anim. Feed Sci. Technol. 49 (1994) 25-35
    • (1994) Anim. Feed Sci. Technol. , vol.49 , pp. 25-35
    • Messman, M.A.1    Weiss, W.P.2
  • 23
    • 0000870544 scopus 로고
    • Kinetics of invertase action
    • Michaelis L., and Menten M.L. Kinetics of invertase action. Biochem. J. 49 (1913) 333-369
    • (1913) Biochem. J. , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.L.2
  • 24
    • 0021031123 scopus 로고
    • Rates of proteolysis in the rumen of the soluble proteins casein Fraction I (18S) leaf protein bovine serum albumin and bovine submaxillary mucoprotein
    • Nugent J.H.A., Jones W.T., and Jordan D.J. Rates of proteolysis in the rumen of the soluble proteins casein Fraction I (18S) leaf protein bovine serum albumin and bovine submaxillary mucoprotein. Br. J. Nutr. 50 (1983) 357-368
    • (1983) Br. J. Nutr. , vol.50 , pp. 357-368
    • Nugent, J.H.A.1    Jones, W.T.2    Jordan, D.J.3
  • 26
    • 0016358276 scopus 로고
    • Mechanism of action of the toxic lectins abrin and ricin
    • Olsnes S., Refsnes K., and Pihl A. Mechanism of action of the toxic lectins abrin and ricin. Nature 249 (1974) 627-631
    • (1974) Nature , vol.249 , pp. 627-631
    • Olsnes, S.1    Refsnes, K.2    Pihl, A.3
  • 27
    • 33646320949 scopus 로고
    • Estimation of protein degradability in the rumen from incubation measurements weighted according to rate of passage
    • Orskov E.R., and Mcdonald I. Estimation of protein degradability in the rumen from incubation measurements weighted according to rate of passage. J. Agric. Sci. 92 (1979) 499-503
    • (1979) J. Agric. Sci. , vol.92 , pp. 499-503
    • Orskov, E.R.1    Mcdonald, I.2
  • 28
    • 0005145541 scopus 로고
    • Protein metabolism of nutrition animals
    • Church D.C. (Ed), Prentice Hall, Englewood Cliffs, NJ
    • Owens F.N., and Zinn R. Protein metabolism of nutrition animals. In: Church D.C. (Ed). The Ruminant Animal: Digestive Physiology and Nutrition (1988), Prentice Hall, Englewood Cliffs, NJ 227-249
    • (1988) The Ruminant Animal: Digestive Physiology and Nutrition , pp. 227-249
    • Owens, F.N.1    Zinn, R.2
  • 29
    • 0033105962 scopus 로고    scopus 로고
    • Protein purification from polyacrylamide gels by sonication extraction
    • Retamal C.A., Thiebaut P., and Alves E.W. Protein purification from polyacrylamide gels by sonication extraction. Anal. Biochem. 268 (1999) 15-20
    • (1999) Anal. Biochem. , vol.268 , pp. 15-20
    • Retamal, C.A.1    Thiebaut, P.2    Alves, E.W.3
  • 30
    • 0028417668 scopus 로고
    • Electrophoretic analysis of ruminal degradability of corn proteins
    • Romagnolo D.C., Polan C.E., and Barbeau W.E. Electrophoretic analysis of ruminal degradability of corn proteins. J. Dairy Sci. 77 (1994) 1093-1099
    • (1994) J. Dairy Sci. , vol.77 , pp. 1093-1099
    • Romagnolo, D.C.1    Polan, C.E.2    Barbeau, W.E.3
  • 32
    • 0001329109 scopus 로고
    • Proteolytic enzymes and their inhibitors in plants
    • Ryan C.A. Proteolytic enzymes and their inhibitors in plants. Annu. Rev. Plant Physiol. 24 (1973) 173-196
    • (1973) Annu. Rev. Plant Physiol. , vol.24 , pp. 173-196
    • Ryan, C.A.1
  • 33
    • 38949170551 scopus 로고    scopus 로고
    • Effects of microwave irradiation on ruminal dry matter, protein and starch degradation characteristics of barley grain
    • Sadeghi A.A., and Shawrang P. Effects of microwave irradiation on ruminal dry matter, protein and starch degradation characteristics of barley grain. Anim. Feed Sci. Technol. 141 (2008) 184-194
    • (2008) Anim. Feed Sci. Technol. , vol.141 , pp. 184-194
    • Sadeghi, A.A.1    Shawrang, P.2
  • 34
    • 77949913098 scopus 로고
    • Resposta comparativa de bovinos jovens em confinamento, ao farelo de mamona adubo e lex protéico (Traduction: comparative response of young cattle in feedlot, to castorseed meal fertilizer and lex protéico)
    • Sociedade Brasileira de Zootecnia (Brazilian Society Animal Science), Anais... Rio de Janeiro 144-145
    • Santana O.P., Caldas G.C., and Araújo P.E.S. Resposta comparativa de bovinos jovens em confinamento, ao farelo de mamona adubo e lex protéico (Traduction: comparative response of young cattle in feedlot, to castorseed meal fertilizer and lex protéico). Reunião Anual da Sociedade Brasileira de Zootecnia (Annual Meeting of Brazilian Society Animal Science), Rio de Janeiro, Brazil. eighth ed. (1971), Sociedade Brasileira de Zootecnia (Brazilian Society Animal Science), Anais... Rio de Janeiro 144-145
    • (1971) Reunião Anual da Sociedade Brasileira de Zootecnia (Annual Meeting of Brazilian Society Animal Science), Rio de Janeiro, Brazil. eighth ed.
    • Santana, O.P.1    Caldas, G.C.2    Araújo, P.E.S.3
  • 36
    • 0030077077 scopus 로고    scopus 로고
    • Use of sodium dodecyl sulfate polyacrylamide gel electrophoresis to measure degradation of soluble soybean proteins by Prevotella ruminocola GA33 or mixed ruminal microbes in vitro
    • Schwingel W.R., and Bates D.B. Use of sodium dodecyl sulfate polyacrylamide gel electrophoresis to measure degradation of soluble soybean proteins by Prevotella ruminocola GA33 or mixed ruminal microbes in vitro. J. Anim. Sci. 74 (1996) 475-482
    • (1996) J. Anim. Sci. , vol.74 , pp. 475-482
    • Schwingel, W.R.1    Bates, D.B.2
  • 37
    • 77952891222 scopus 로고    scopus 로고
    • Scientific Opinion of the Panel on Contaminants in the Food Chain on a request from the European Commission on ricin (from Ricinus communis) as undesirable substances in animal feed
    • SOPCF. Scientific Opinion of the Panel on Contaminants in the Food Chain on a request from the European Commission on ricin (from Ricinus communis) as undesirable substances in animal feed. EFSA J. 726 (2008) 1-38
    • (2008) EFSA J. , vol.726 , pp. 1-38
    • SOPCF1
  • 38
    • 0023697287 scopus 로고
    • Monitoring the fate of dietary proteins in rumen fluid using gel electrophoresis
    • Spencer D., Higgins T.J.V., Freer M., Dove H., and Coombe J.B. Monitoring the fate of dietary proteins in rumen fluid using gel electrophoresis. Br. J. Nutr. 60 (1988) 241-247
    • (1988) Br. J. Nutr. , vol.60 , pp. 241-247
    • Spencer, D.1    Higgins, T.J.V.2    Freer, M.3    Dove, H.4    Coombe, J.B.5
  • 39
    • 0028509418 scopus 로고
    • Evaluation of chemical and physical properties of feeds that affect protein metabolism in the rumen
    • Stern M.D., Varga G.A., Clark J.H., Firkins J.L., Huber J.T., and Palmquist D.L. Evaluation of chemical and physical properties of feeds that affect protein metabolism in the rumen. J. Dairy Sci. 77 (1994) 2762-2786
    • (1994) J. Dairy Sci. , vol.77 , pp. 2762-2786
    • Stern, M.D.1    Varga, G.A.2    Clark, J.H.3    Firkins, J.L.4    Huber, J.T.5    Palmquist, D.L.6
  • 40
    • 0031180561 scopus 로고    scopus 로고
    • Analysis of lupin seed protein digestibility using gel electrophoresis and immunoblots
    • Tai H.H., and Bush R.S. Analysis of lupin seed protein digestibility using gel electrophoresis and immunoblots. J. Anim. Sci. 75 (1997) 1934-1940
    • (1997) J. Anim. Sci. , vol.75 , pp. 1934-1940
    • Tai, H.H.1    Bush, R.S.2
  • 41
    • 0031491335 scopus 로고    scopus 로고
    • Crossimmunity by the seeds of Abrus precatorius and Ricinus communis in cattle
    • (in Portuguese, with English abstract)
    • Tokarnia C.H., and Dobereiner J. Crossimmunity by the seeds of Abrus precatorius and Ricinus communis in cattle. Pesq. Vet. Bras. 17 (1997) 25-35 (in Portuguese, with English abstract)
    • (1997) Pesq. Vet. Bras. , vol.17 , pp. 25-35
    • Tokarnia, C.H.1    Dobereiner, J.2
  • 42
    • 0002634307 scopus 로고    scopus 로고
    • Metabolism of nitrogen-containing compounds
    • Hobson P.N., and Stewart C.S. (Eds), Chapmann and Hall, London, UK
    • Wallace R.J., Onodera R., and Cotta M.A. Metabolism of nitrogen-containing compounds. In: Hobson P.N., and Stewart C.S. (Eds). The Rumen Microbial Ecosystem. second ed. (1997), Chapmann and Hall, London, UK 283-328
    • (1997) The Rumen Microbial Ecosystem. second ed. , pp. 283-328
    • Wallace, R.J.1    Onodera, R.2    Cotta, M.A.3
  • 43
    • 0022778417 scopus 로고
    • Effect of acid and alkali treatment of soybean meal on nitrogen utilization by ruminants
    • Waltz D.M., and Loerch S.C. Effect of acid and alkali treatment of soybean meal on nitrogen utilization by ruminants. J. Anim. Sci. 63 (1986) 879-887
    • (1986) J. Anim. Sci. , vol.63 , pp. 879-887
    • Waltz, D.M.1    Loerch, S.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.