메뉴 건너뛰기




Volumn 70, Issue 11, 2006, Pages 2620-2626

7S globulins from Phaseolus vulgaris L.: Impact of structural aspects on the nutritional quality

Author keywords

7S globulin; FT IR; Phaseolus vulgaris; Protein quality; Structure

Indexed keywords

FOURIER TRANSFORM INFRARED SPECTROSCOPY; NUTRITION; PLANTS (BOTANY); SEED;

EID: 33751422523     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60203     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 0028361114 scopus 로고
    • Structure of phaseolin at 2.2 Å resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins
    • Lawrence, M. C., Izard, T., Beuchat, M., Blagrove, R. J., and Colman, P. M., Structure of phaseolin at 2.2 Å resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. J. Mol. Biol., 238, 748-776 (1994).
    • (1994) J. Mol. Biol. , vol.238 , pp. 748-776
    • Lawrence, M.C.1    Izard, T.2    Beuchat, M.3    Blagrove, R.J.4    Colman, P.M.5
  • 3
    • 0034096545 scopus 로고    scopus 로고
    • The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 Å resolution
    • Ko, T.-P., Day, J., and McPherson, A., The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 Å resolution. Acta Crystallogr., D56, 411-420 (2000).
    • (2000) Acta Crystallogr. , vol.D56 , pp. 411-420
    • Ko, T.-P.1    Day, J.2    McPherson, A.3
  • 5
    • 20144386252 scopus 로고    scopus 로고
    • Molecular modelling of the major peanut allergen Ara h 1 and other homotrimeric allergens of the cupin superfamily: A structural basis for their IgE-binding cross-reactivity
    • Barre, A., Borges, J.-P., and Rougé, P., Molecular modelling of the major peanut allergen Ara h 1 and other homotrimeric allergens of the cupin superfamily: a structural basis for their IgE-binding cross-reactivity. Biochimie, 87, 499-506 (2005).
    • (2005) Biochimie , vol.87 , pp. 499-506
    • Barre, A.1    Borges, J.-P.2    Rougé, P.3
  • 6
    • 84985257187 scopus 로고
    • Structure-digestibility relationship of legume 7S proteins
    • Deshpande, S. S., and Damodaran, S. D., Structure-digestibility relationship of legume 7S proteins. J. Food Sci., 54, 108-113 (1989).
    • (1989) J. Food Sci. , vol.54 , pp. 108-113
    • Deshpande, S.S.1    Damodaran, S.D.2
  • 9
    • 27144501099 scopus 로고    scopus 로고
    • Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by Fourier transform infrared spectroscopy and differential scanning calorimetry
    • Choi, S. M., and Ma, C. Y., Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by Fourier transform infrared spectroscopy and differential scanning calorimetry. J. Agric. Food Chem., 53, 8046-8053 (2005).
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 8046-8053
    • Choi, S.M.1    Ma, C.Y.2
  • 10
    • 27544467437 scopus 로고    scopus 로고
    • Conformational study of globulin from rice (Oryza sativa) seeds by Fourier-transform infrared spectroscopy
    • Ellepola, S. W., Choi, S. M., and Ma, C. Y., Conformational study of globulin from rice (Oryza sativa) seeds by Fourier-transform infrared spectroscopy. Int. J. Biol. Macromol., 37, 12-20 (2005).
    • (2005) Int. J. Biol. Macromol. , vol.37 , pp. 12-20
    • Ellepola, S.W.1    Choi, S.M.2    Ma, C.Y.3
  • 11
    • 0003896304 scopus 로고
    • Association of Official Analytical Chemists, Arlington, VA
    • AOAC Official Methods of Analysis, 15th ed., Association of Official Analytical Chemists, Arlington, VA (1990).
    • (1990) AOAC Official Methods of Analysis, 15th Ed.
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 84987301218 scopus 로고
    • Chromatography of amino acids on sulphonated polystyrene resins
    • Moore, S., Spackman, D. M., and Stein, W. H., Chromatography of amino acids on sulphonated polystyrene resins. Anal. Chem., 30, 1185-1190 (1958).
    • (1958) Anal. Chem. , vol.30 , pp. 1185-1190
    • Moore, S.1    Spackman, D.M.2    Stein, W.H.3
  • 14
    • 77049171228 scopus 로고
    • Chromatographic determination of cystine as cysteic acid
    • Schram, E., Moore, S., and Bigwood, E. J., Chromatographic determination of cystine as cysteic acid. Biochem. J., 57, 33-37 (1954).
    • (1954) Biochem. J. , vol.57 , pp. 33-37
    • Schram, E.1    Moore, S.2    Bigwood, E.J.3
  • 15
    • 84985409711 scopus 로고
    • Tryptophan determination of food proteins by HPLC after alkaline hydrolysis
    • Nielsen, H. K., and Hurrell, R. F., Tryptophan determination of food proteins by HPLC after alkaline hydrolysis. J. Sci. Food Agric., 36, 893-907 (1985).
    • (1985) J. Sci. Food Agric. , vol.36 , pp. 893-907
    • Nielsen, H.K.1    Hurrell, R.F.2
  • 17
  • 18
    • 11244328652 scopus 로고    scopus 로고
    • Heat-induced denaturation impairs digestibility of legume (Phaseolus vulgaris L. and Vicia faba L.) 7S and 11S globulins in the small intestine of rat
    • Carbonaro, M., Grant, G., and Cappelloni, M., Heat-induced denaturation impairs digestibility of legume (Phaseolus vulgaris L. and Vicia faba L.) 7S and 11S globulins in the small intestine of rat. J. Sci. Food Agric., 85, 65-72 (2005).
    • (2005) J. Sci. Food Agric. , vol.85 , pp. 65-72
    • Carbonaro, M.1    Grant, G.2    Cappelloni, M.3
  • 19
    • 49349130487 scopus 로고
    • Legumin and vicilin, storage proteins of legume seeds
    • Derbyshire, E., Wright, D. J., 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
  • 21
    • 0001603321 scopus 로고
    • In-vitro protein and sulphur amino acid availability as a measure of bean protein quality
    • Marletta, L., Carbonaro, M., and Carnovale, E., In-vitro protein and sulphur amino acid availability as a measure of bean protein quality. J. Sci. Food Agric., 59, 497-504 (1992).
    • (1992) J. Sci. Food Agric. , vol.59 , pp. 497-504
    • Marletta, L.1    Carbonaro, M.2    Carnovale, E.3
  • 22
    • 0032792453 scopus 로고    scopus 로고
    • Heat-induced aggregation of Phaseolus vulgaris L. proteins: An electron spin resonance study
    • Carbonaro, M., Nicoli, S., and Musci, G., Heat-induced aggregation of Phaseolus vulgaris L. proteins: an electron spin resonance study. J. Agric. Food Chem., 47, 2188-2192 (1999).
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 2188-2192
    • Carbonaro, M.1    Nicoli, S.2    Musci, G.3
  • 23
    • 0034116666 scopus 로고    scopus 로고
    • Perspectives into factors limiting in vivo digestion of legume proteins: Antinutritional compounds or storage proteins?
    • Carbonaro, M., Grant, G., Cappelloni, M., and Pusztai, A., Perspectives into factors limiting in vivo digestion of legume proteins: antinutritional compounds or storage proteins? J. Agric. Food Chem., 48, 742-749 (2000).
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 742-749
    • Carbonaro, M.1    Grant, G.2    Cappelloni, M.3    Pusztai, A.4
  • 24
    • 0000560962 scopus 로고
    • Protein solubility of raw and cooked beans (Phaseolus vulgaris): Role of the basic residues
    • Carbonaro, M., Vecchini, P., and Carnovale, E., Protein solubility of raw and cooked beans (Phaseolus vulgaris): role of the basic residues. J. Agric. Food Chem., 41, 1169-1175 (1993).
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 1169-1175
    • Carbonaro, M.1    Vecchini, P.2    Carnovale, E.3
  • 25
    • 4444344985 scopus 로고    scopus 로고
    • Heat-induced secondary structure and conformation of bovine serum albumin investigated by Fourier transform infrared spectroscopy
    • Murayama, K., and Tomida, M., Heat-induced secondary structure and conformation of bovine serum albumin investigated by Fourier transform infrared spectroscopy. Biochemistry, 43, 11526-11532 (2004).
    • (2004) Biochemistry , vol.43 , pp. 11526-11532
    • Murayama, K.1    Tomida, M.2
  • 26
    • 0032189531 scopus 로고    scopus 로고
    • Salt-soluble seed globulins of dicotyledonous and monocotyledonous plants II. Structural characterization
    • Marcone, F. M., Kakuda, Y., and Yada, R. Y., Salt-soluble seed globulins of dicotyledonous and monocotyledonous plants II. Structural characterization. Food Chem., 63, 265-274 (1998).
    • (1998) Food Chem. , vol.63 , pp. 265-274
    • Marcone, F.M.1    Kakuda, Y.2    Yada, R.Y.3
  • 27
    • 0036335312 scopus 로고    scopus 로고
    • Characterization of globulin from Phaseolus angularis (red bean)
    • Meng, G., and Ma, C.-Y., Characterization of globulin from Phaseolus angularis (red bean). Int. J. Food Sci. Technol., 37, 687-695 (2002).
    • (2002) Int. J. Food Sci. Technol. , vol.37 , pp. 687-695
    • Meng, G.1    Ma, C.-Y.2
  • 28
    • 0033514289 scopus 로고    scopus 로고
    • Thermal and pH-induced conformational changes of a β-sheet protein monitored by infrared spectroscopy
    • Chehin, R., Iloro, I., Marcos, M. J., Villar, E., Shnyrov, V. L., and Arrondo, J. L. R., Thermal and pH-induced conformational changes of a β-sheet protein monitored by infrared spectroscopy. Biochemistry, 38, 1525-1530 (1999).
    • (1999) Biochemistry , vol.38 , pp. 1525-1530
    • Chehin, R.1    Iloro, I.2    Marcos, M.J.3    Villar, E.4    Shnyrov, V.L.5    Arrondo, J.L.R.6
  • 29
    • 33845471438 scopus 로고
    • Heat-induced interactions between soybean proteins: Preferential association of 11S basic subunits and β-subunits of 7S
    • Utsumi, S., Damodaran, S., and Kinsella, J. E., Heat-induced interactions between soybean proteins: preferential association of 11S basic subunits and β-subunits of 7S. J. Agric. Food Chem., 32, 1406-1412 (1984).
    • (1984) J. Agric. Food Chem. , vol.32 , pp. 1406-1412
    • Utsumi, S.1    Damodaran, S.2    Kinsella, J.E.3
  • 30
    • 33751398084 scopus 로고    scopus 로고
    • A spectroscopic study on the metal-binding ability of gastrointestinal peptides from Phaseolus vulgaris L.: A comparison with whole milk
    • AEP, Paris
    • Carbonaro, M., Iametti, S., Mattera, M., and Bonomi, F., A spectroscopic study on the metal-binding ability of gastrointestinal peptides from Phaseolus vulgaris L.: a comparison with whole milk. Proc. "5th European Conference on Grain Legumes," AEP, Paris, pp. 25-26 (2004).
    • (2004) Proc. "5th European Conference on Grain Legumes" , pp. 25-26
    • Carbonaro, M.1    Iametti, S.2    Mattera, M.3    Bonomi, F.4
  • 31
    • 0031405335 scopus 로고    scopus 로고
    • Effects of short-term feeding of rats with a highly purified phaseolin preparation
    • Santoro, L. G., Grant, G., and Pusztai, A., Effects of short-term feeding of rats with a highly purified phaseolin preparation. Plant Foods Hum. Nutr., 51, 61-70 (1997).
    • (1997) Plant Foods Hum. Nutr. , vol.51 , pp. 61-70
    • Santoro, L.G.1    Grant, G.2    Pusztai, A.3
  • 32
    • 0037125116 scopus 로고    scopus 로고
    • Nutritional utilization by the rat of diets based on lentil (Lens culinaris) seed meal or its fractions
    • Cuadrado, C., Grant, G., Rubio, L. A., Muzquiz, M., Bardocz, S., and Pusztai, A., Nutritional utilization by the rat of diets based on lentil (Lens culinaris) seed meal or its fractions. J. Agric. Food Chem., 50, 4371-4376 (2002).
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 4371-4376
    • Cuadrado, C.1    Grant, G.2    Rubio, L.A.3    Muzquiz, M.4    Bardocz, S.5    Pusztai, A.6
  • 33
    • 0342396907 scopus 로고
    • Comparative study on bioavailability of different soybean antigens
    • Hajos, G., Gelencser, E., and Polgar, M., Comparative study on bioavailability of different soybean antigens. Ber. Bundesforshungsanst. Ernaehr., 1, 44-52 (1993).
    • (1993) Ber. Bundesforshungsanst. Ernaehr. , vol.1 , pp. 44-52
    • Hajos, G.1    Gelencser, E.2    Polgar, M.3
  • 34
    • 0033582479 scopus 로고    scopus 로고
    • Heat-induced conformational changes of Ara h1, a major peanut allergen, do not affect its allergenic properties
    • Koppelman, S. J., Bruijnzeel-Koomen, C. A. F. M., Hessing, M., and de Jongh, H. H. J., Heat-induced conformational changes of Ara h1, a major peanut allergen, do not affect its allergenic properties. J. Biol. Chem., 274, 4770-4777 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 4770-4777
    • Koppelman, S.J.1    Bruijnzeel-Koomen, C.A.F.M.2    Hessing, M.3    De Jongh, H.H.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.