메뉴 건너뛰기




Volumn 80, Issue 4, 2000, Pages 513-521

The use of anti-soya globulin antisera in investigating soya digestion in vivo

Author keywords

Digestion; Globulins; Polyclonal antibodies; Soya

Indexed keywords

ANTIBODY DETECTION; ANTIBODY SPECIFICITY; BETA CONGLYCININ; DIGESTION; ENZYME LINKED IMMUNOSORBENT ASSAY; ENZYMIC HYDROLYSIS; GLOBULIN; GLYCININ; IN VIVO STUDY; POLYCLONAL ANTIBODY; PROTEIN BINDING; PROTEIN HYDROLYSIS; RAT; SDS POLYACRYLAMIDE GEL ELECTROPHORESIS; SOYBEAN; THERMOSTABILITY;

EID: 0034009152     PISSN: 00225142     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0010(200003)80:4<513::AID-JSFA562>3.0.CO;2-N     Document Type: Article
Times cited : (32)

References (35)
  • 1
    • 0343310841 scopus 로고
    • Effects of dietary antigens on health, performance and immune system of calves and piglets
    • Ed by van der Poel AFP, Huisman J and Saini HS. Wageningen Piers, Wageningen
    • Lalles JP, Salmon H, Bakker NPH and Tolman GH, Effects of dietary antigens on health, performance and immune system of calves and piglets, in Recent Advances of Research in Agricultural Factors in Legume Seeds, Ed by van der Poel AFP, Huisman J and Saini HS. Wageningen Piers, Wageningen, pp 253-270 (1993).
    • (1993) Recent Advances of Research in Agricultural Factors in Legume Seeds , pp. 253-270
    • Lalles, J.P.1    Salmon, H.2    Bakker, N.P.H.3    Tolman, G.H.4
  • 2
    • 0040493294 scopus 로고
    • Effects of soya-bean products on digestive processes in the gastrointestinal tract of preruminant calves
    • Sissons JW, Effects of soya-bean products on digestive processes in the gastrointestinal tract of preruminant calves. Proc Nutr Soc 41:53-61 (1982).
    • (1982) Proc Nutr Soc , vol.41 , pp. 53-61
    • Sissons, J.W.1
  • 4
    • 0019154211 scopus 로고
    • Protein digestibility of the same protein preparations by human and rat assays and by in vitro enzymic digestion methods
    • Bodwell CE, Satterlee LD and Hackler LR, Protein digestibility of the same protein preparations by human and rat assays and by in vitro enzymic digestion methods. Am J Clin Nutr 33:677-686 (1980).
    • (1980) Am J Clin Nutr , vol.33 , pp. 677-686
    • Bodwell, C.E.1    Satterlee, L.D.2    Hackler, L.R.3
  • 5
    • 0022523218 scopus 로고
    • Digestion of milk, fish and soya bean protein in the preruminant calf: Flow of digesta, apparent digestibility at the end of the ileum and amino acid composition of ileal digesta
    • Guilloteau P, Toullec R, Grongnet JF, Patureau-Mirand P and Prugnaud J, Digestion of milk, fish and soya bean protein in the preruminant calf: flow of digesta, apparent digestibility at the end of the ileum and amino acid composition of ileal digesta. Br J Nutr 55:571-592 (1986).
    • (1986) Br J Nutr , vol.55 , pp. 571-592
    • Guilloteau, P.1    Toullec, R.2    Grongnet, J.F.3    Patureau-Mirand, P.4    Prugnaud, J.5
  • 6
    • 0024808904 scopus 로고
    • Digestion des proteins du pois et du soya chez le veau preruminant. II. Digestibilité apparente à la fui de l'iléon et du tube digestif
    • Nunes do Prado I, Toullec R, Guilloteau P and Gueguen J, Digestion des proteins du pois et du soya chez le veau preruminant. II. Digestibilité apparente à la fui de l'iléon et du tube digestif. Reprod Nutr Develop 29:425-439 (1989).
    • (1989) Reprod Nutr Develop , vol.29 , pp. 425-439
    • Nunes Do Prado, I.1    Toullec, R.2    Guilloteau, P.3    Gueguen, J.4
  • 7
    • 0001600391 scopus 로고
    • Digestion of soybean globulins, glycinin, α-conglycinin and β-conglycinin in the preruminant and ruminant calf
    • Tukur HM, Lalles JP, Mathis C, Caugant I and Toullec R, Digestion of soybean globulins, glycinin, α-conglycinin and β-conglycinin in the preruminant and ruminant calf. Can J Anim Sci 73:891-905 (1993).
    • (1993) Can J Anim Sci , vol.73 , pp. 891-905
    • Tukur, H.M.1    Lalles, J.P.2    Mathis, C.3    Caugant, I.4    Toullec, R.5
  • 8
    • 0019588886 scopus 로고
    • Digestion in the pig between 7 and 35d of age. 6. The digestion of hydrolysed milk and soya bean proteins
    • Leibholz J, Digestion in the pig between 7 and 35d of age. 6. The digestion of hydrolysed milk and soya bean proteins. Br J Nutr 46:59-69 (1981).
    • (1981) Br J Nutr , vol.46 , pp. 59-69
    • Leibholz, J.1
  • 9
    • 0020160594 scopus 로고
    • Artificial rearing of pigs. 12. Effect of replacement of dried skim-milk by either a soya-protein isolate or concentrate on the performance of the pigs and digestion of protein
    • Newport MJ and Keal HD, Artificial rearing of pigs. 12. Effect of replacement of dried skim-milk by either a soya-protein isolate or concentrate on the performance of the pigs and digestion of protein. Br J Nutr 48:89-96 (1982).
    • (1982) Br J Nutr , vol.48 , pp. 89-96
    • Newport, M.J.1    Keal, H.D.2
  • 10
  • 11
    • 84985154147 scopus 로고
    • Legume toxins in relation to protein digestibility: A review
    • Leiner IE, Legume toxins in relation to protein digestibility: a review. J Food Sci 41:1076-1081 (1976).
    • (1976) J Food Sci , vol.41 , pp. 1076-1081
    • Leiner, I.E.1
  • 12
    • 84987319367 scopus 로고
    • In vitro digestibility of dry bean (Phaseolus vulgaris L.) proteins. The role of heat-stable proteinase inhibitors
    • Deshpande SS and Nielsen SS, In vitro digestibility of dry bean (Phaseolus vulgaris L.) proteins. The role of heat-stable proteinase inhibitors. J Food Sci 52:1330-1334 (1987).
    • (1987) J Food Sci , vol.52 , pp. 1330-1334
    • Deshpande, S.S.1    Nielsen, S.S.2
  • 13
    • 0019618248 scopus 로고
    • Composition and digestibility of albumins, globulins, and glutelins from Phaseolus vulgaris
    • Marquez UML and Lajolo FM, Composition and digestibility of albumins, globulins, and glutelins from Phaseolus vulgaris. J Agric Food Chem 29:1068-1074 (1981).
    • (1981) J Agric Food Chem , vol.29 , pp. 1068-1074
    • Marquez, U.M.L.1    Lajolo, F.M.2
  • 14
    • 0343046189 scopus 로고
    • Digestibility and proteinase inhibitory action of a kidney bean phaseolin
    • Seidl D, Jaffe M and Jaffe WG, Digestibility and proteinase inhibitory action of a kidney bean phaseolin. J Agric Food Chem 17:1318-1321 (1969).
    • (1969) J Agric Food Chem , vol.17 , pp. 1318-1321
    • Seidl, D.1    Jaffe, M.2    Jaffe, W.G.3
  • 15
    • 75949157210 scopus 로고
    • A pepsin-pancreatin digest index of protein quality evaluation
    • Akeson WR and Stahmann MA, A pepsin-pancreatin digest index of protein quality evaluation. J Nutr 83:257-261 (1964).
    • (1964) J Nutr , vol.83 , pp. 257-261
    • Akeson, W.R.1    Stahmann, M.A.2
  • 16
    • 0015611830 scopus 로고
    • Measurement of digestibility of alfalfa protein concentrates by in vivo and in vitro methods
    • Saunders RM, Connor MA, Booth AN, Bickoff EM and Kohler GO, Measurement of digestibility of alfalfa protein concentrates by in vivo and in vitro methods. J Nutr 103:530-535 (1973).
    • (1973) J Nutr , vol.103 , pp. 530-535
    • Saunders, R.M.1    Connor, M.A.2    Booth, A.N.3    Bickoff, E.M.4    Kohler, G.O.5
  • 17
    • 0025937718 scopus 로고
    • Protein digestibility in vitro methods of assessment
    • Swaisgood HE and Catignani GL, Protein digestibility in vitro methods of assessment. Adv Food Nutr Res 35:185-236(1991).
    • (1991) Adv Food Nutr Res , vol.35 , pp. 185-236
    • Swaisgood, H.E.1    Catignani, G.L.2
  • 18
    • 0017021691 scopus 로고
    • Effect of heat, amylase, and disulphide bond cleavage on the in vitro digestibility of soybean proteins
    • Boonvisut S and Whitaker JR, Effect of heat, amylase, and disulphide bond cleavage on the in vitro digestibility of soybean proteins. J Agric Food Chem 24:1130-1135 (1976).
    • (1976) J Agric Food Chem , vol.24 , pp. 1130-1135
    • Boonvisut, S.1    Whitaker, J.R.2
  • 20
    • 0039280712 scopus 로고
    • Differences in the degradation m vivo and in vitro of phaseolin, the major storage protein of Phaseolus vulgaris seeds
    • Santoro LG, Grant G and Pusztai A, Differences in the degradation m vivo and in vitro of phaseolin, the major storage protein of Phaseolus vulgaris seeds. Biochem Soc Trans 16:612-613 (1988).
    • (1988) Biochem Soc Trans , vol.16 , pp. 612-613
    • Santoro, L.G.1    Grant, G.2    Pusztai, A.3
  • 21
    • 49349130487 scopus 로고
    • Legumin and vicilin storage proteins of legume seeds
    • Derbyshire E, Wright DJ and Boulter D, Legumin and vicilin storage proteins of legume seeds. Phytochemistry 15:3-24 (1976).
    • (1976) Phytochemistry , vol.15 , pp. 3-24
    • Derbyshire, E.1    Wright, D.J.2    Boulter, D.3
  • 22
    • 0043152270 scopus 로고
    • Purification of the 11S component of soybean protein
    • Eldridge AC and Wolf WJ, Purification of the 11S component of soybean protein. Cereal Chem 44:645-668 (1967).
    • (1967) Cereal Chem , vol.44 , pp. 645-668
    • Eldridge, A.C.1    Wolf, W.J.2
  • 23
    • 0017019007 scopus 로고
    • Major proteins of soybean seeds. Straightforward fractionation and their characterisation
    • Thanh VH and Shibasaki K, Major proteins of soybean seeds. Straightforward fractionation and their characterisation. J Agric Food Chem 24:1117-1121 (1976).
    • (1976) J Agric Food Chem , vol.24 , pp. 1117-1121
    • Thanh, V.H.1    Shibasaki, K.2
  • 24
    • 0022853178 scopus 로고
    • Protocol for purification of pea storage proteins and characterisation of their aggregation state
    • Lambert N, Chambers SJ, Phalp M and Wright DJ, Protocol for purification of pea storage proteins and characterisation of their aggregation state. Biochem Soc Trans 14:1186-1188 (1986).
    • (1986) Biochem Soc Trans , vol.14 , pp. 1186-1188
    • Lambert, N.1    Chambers, S.J.2    Phalp, M.3    Wright, D.J.4
  • 25
    • 0002745151 scopus 로고
    • Characterisation of polyclonal and monoclonal antibodies against glycinin (11S storage protein) from soya (Glycine max)
    • Carter JM, Lee HA, Mills ENC, Lambert N, Chan HW-S and Morgan MRA, Characterisation of polyclonal and monoclonal antibodies against glycinin (11S storage protein) from soya (Glycine max). J Sci Food Agric 51:75-82 (1992).
    • (1992) J Sci Food Agric , vol.51 , pp. 75-82
    • Carter, J.M.1    Lee, H.A.2    Mills, E.N.C.3    Lambert, N.4    Hw-S, C.5    Morgan, M.R.A.6
  • 26
    • 0001289346 scopus 로고
    • The effect of thermal and proteolytic processing on glycinin, the 11S globulin of soya (Glycine max) - A study utilising monoclonal and polyclonal antibodies
    • Plumb GW, Mills ENC, Talton MJ, D'Ursel CCM, Lambert N and Morgan MRA, The effect of thermal and proteolytic processing on glycinin, the 11S globulin of soya (Glycine max) - a study utilising monoclonal and polyclonal antibodies. J Agric Food Chem 42:834-840 (1994).
    • (1994) J Agric Food Chem , vol.42 , pp. 834-840
    • Plumb, G.W.1    Mills, E.N.C.2    Talton, M.J.3    D'Ursel, C.C.M.4    Lambert, N.5    Morgan, M.R.A.6
  • 27
    • 0000584163 scopus 로고    scopus 로고
    • Improved curve fitting, parallelism testing, characterisation of sensitivity and specificity, validation and optimisation for radioligand assays
    • Radioimmunoassays and related procedures in medicine
    • Rodbard D, Munoon P and Delean A, Improved curve fitting, parallelism testing, characterisation of sensitivity and specificity, validation and optimisation for radioligand assays. In: Radioimmunoassays and related procedures in medicine, Int At Energ Auth, pp 469-514.
    • Int At Energ Auth , pp. 469-514
    • Rodbard, D.1    Munoon, P.2    Delean, A.3
  • 28
    • 0028343649 scopus 로고
    • The elimination of keratin artifacts in immunoblots probed with polyclonal antibodies
    • Berube B, Coutu L, LeFieure L, Begin S, Dupont H and Sullivan R, The elimination of keratin artifacts in immunoblots probed with polyclonal antibodies. Anal Biochem 217:331-333 (1994).
    • (1994) Anal Biochem , vol.217 , pp. 331-333
    • Berube, B.1    Coutu, L.2    LeFieure, L.3    Begin, S.4    Dupont, H.5    Sullivan, R.6
  • 30
    • 84954946891 scopus 로고
    • Degradation sequence of glycinin by tryptic hydrolysis
    • Kamata Y and Shibasaki K, Degradation sequence of glycinin by tryptic hydrolysis. Agric Biol Chem 42:2103-2109 (1978).
    • (1978) Agric Biol Chem , vol.42 , pp. 2103-2109
    • Kamata, Y.1    Shibasaki, K.2
  • 32
    • 0001394545 scopus 로고
    • The globulin seed storage proteins of flowering plants are derived from two ancestral genes
    • Borroto K and Dure L, The globulin seed storage proteins of flowering plants are derived from two ancestral genes. Plant Mol Biol 8:113-131 (1987).
    • (1987) Plant Mol Biol , vol.8 , pp. 113-131
    • Borroto, K.1    Dure, L.2
  • 33
    • 0001409703 scopus 로고
    • Limited proteolysis of soyabean beta-conglycinin
    • Kamata Y, Otsuka S, Sato M and Shubaki K, Limited proteolysis of soyabean beta-conglycinin. Agric Biol Chem 46:2829-2834 (1982).
    • (1982) Agric Biol Chem , vol.46 , pp. 2829-2834
    • Kamata, Y.1    Otsuka, S.2    Sato, M.3    Shubaki, K.4
  • 34
    • 0015797337 scopus 로고
    • Protein digestion in human intestine as reflected in luminal, mucosal and plasma amino acid concentrations after meals
    • Adibi SA and Mercer DW, Protein digestion in human intestine as reflected in luminal, mucosal and plasma amino acid concentrations after meals. J Clin Imest 52:1586-1594 (1973).
    • (1973) J Clin Imest , vol.52 , pp. 1586-1594
    • Adibi, S.A.1    Mercer, D.W.2
  • 35
    • 0029844186 scopus 로고    scopus 로고
    • Limited proteolysis of β-conglycinin and glycinin, the 7S and 11S storage globulins from soybean (Glycine max (L.) Merr.). Structural and evolutionary implications
    • Shutov AD, Kakhovskaya IA, Bastrygina AS, Bulmaga VP, Horstman C and Muntz K, Limited proteolysis of β-conglycinin and glycinin, the 7S and 11S storage globulins from soybean (Glycine max (L.) Merr.). Structural and evolutionary implications. Eur J Biochem 241:221-228 (1996).
    • (1996) Eur J Biochem , vol.241 , pp. 221-228
    • Shutov, A.D.1    Kakhovskaya, I.A.2    Bastrygina, A.S.3    Bulmaga, V.P.4    Horstman, C.5    Muntz, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.