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Volumn 43, Issue 5, 2010, Pages 1494-1504

Functional and molecular properties of calcium precipitated soy glycinin and the effect of glycation with κ-carrageenan

Author keywords

Functional properties; Glycation; Heat denaturation; Protein structure; Salts; Soy glycinin

Indexed keywords

FUNCTIONAL PROPERTIES; GLYCATION; GLYCININ; HEAT DENATURATION; PROTEIN STRUCTURE; PROTEIN STRUCTURES;

EID: 77953912095     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2010.04.005     Document Type: Article
Times cited : (35)

References (85)
  • 1
    • 77953911392 scopus 로고
    • Assn. of Official Analytical Chemists. Method 992.15. In: Official methods of analysis of Assn. of Official Analytical Chemists. Washington, DC.
    • Assn. of Official Analytical Chemists. Method 992.15 (1995). In: Official methods of analysis of Assn. of Official Analytical Chemists. Washington, DC.
    • (1995)
  • 2
    • 77953911630 scopus 로고
    • AACC American Assn. of Cereal Chemistry
    • In: Approved methods of the American Association of Cereal Chemistry. 8th ed. St. Paul, Minn
    • AACC American Assn. of Cereal Chemistry. Method 44-15A. (1983). In: Approved methods of the American Association of Cereal Chemistry. 8th ed. St. Paul, Minn.
    • (1983) Method 44-15A
  • 3
    • 77953917031 scopus 로고    scopus 로고
    • AACC American Assn. of Cereal Chemistry. Method 08-03 In: Approved methods of the American Association of Cereal Chemistry. 8th ed. St. Paul, Minn
    • AACC American Assn. of Cereal Chemistry. Method 08-03 (2003). In: Approved methods of the American Association of Cereal Chemistry. 8th ed. St. Paul, Minn.
    • (2003)
  • 6
    • 0032446301 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of soy protein isolate and effect of succinylation on the functional properties of resulting protein hydrolysates
    • Achouri A., Zhang W., Shiying X. Enzymatic hydrolysis of soy protein isolate and effect of succinylation on the functional properties of resulting protein hydrolysates. Food Research International 1998, 31:617-623.
    • (1998) Food Research International , vol.31 , pp. 617-623
    • Achouri, A.1    Zhang, W.2    Shiying, X.3
  • 8
    • 0000517106 scopus 로고    scopus 로고
    • Comparison of chemical and biopolar-membrane electrochemical acidification for precipitation of soybean proteins
    • Bazinet F., Lamarche F., Ippersiel D. Comparison of chemical and biopolar-membrane electrochemical acidification for precipitation of soybean proteins. Journal of Agriculture and Food Chemistry 1998, 46:2013-2019.
    • (1998) Journal of Agriculture and Food Chemistry , vol.46 , pp. 2013-2019
    • Bazinet, F.1    Lamarche, F.2    Ippersiel, D.3
  • 9
    • 84987309977 scopus 로고
    • Nitrogen solubility of alfalfa protein concentrates as influenced by various factors
    • Betschart A.A. Nitrogen solubility of alfalfa protein concentrates as influenced by various factors. Journal of Food Science 1974, 39:1110-1115.
    • (1974) Journal of Food Science , vol.39 , pp. 1110-1115
    • Betschart, A.A.1
  • 10
    • 0023394761 scopus 로고
    • Effect of calcium chloride on the conformation of proteins: Thermodynamic studies of some model compounds
    • Bhat R., Ahluwalia J.C. Effect of calcium chloride on the conformation of proteins: Thermodynamic studies of some model compounds. International Journal of Peptide and Protein Research 1987, 30(2):145-152.
    • (1987) International Journal of Peptide and Protein Research , vol.30 , Issue.2 , pp. 145-152
    • Bhat, R.1    Ahluwalia, J.C.2
  • 14
    • 0030088058 scopus 로고    scopus 로고
    • Effect of physicochemical factors on the secondary structure of β-lactoglobulin
    • Boye J.I., Ismail A., Alli I. Effect of physicochemical factors on the secondary structure of β-lactoglobulin. Journal of Dairy Research 1996, 63:97-109.
    • (1996) Journal of Dairy Research , vol.63 , pp. 97-109
    • Boye, J.I.1    Ismail, A.2    Alli, I.3
  • 15
    • 0642302370 scopus 로고    scopus 로고
    • Molecular and microstructure studies of thermal denaturation and gelation of β-lactoglobulins A and B
    • Boye J.I., Ma C.Y., Ismail A., Harwalkar V.R. Molecular and microstructure studies of thermal denaturation and gelation of β-lactoglobulins A and B. Journal of Agriculture and Food Chemistry 1997, 45:1608-1618.
    • (1997) Journal of Agriculture and Food Chemistry , vol.45 , pp. 1608-1618
    • Boye, J.I.1    Ma, C.Y.2    Ismail, A.3    Harwalkar, V.R.4
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976, 72:248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler D.M., Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 1986, 25:469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 21
    • 0034921222 scopus 로고    scopus 로고
    • Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar
    • Chevalier F., Chobert J.M., Popineau Y., Nicolas M.G., Haertlé T. Improvement of functional properties of β-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar. International Dairy Journal 2001, 11:145-152.
    • (2001) International Dairy Journal , vol.11 , pp. 145-152
    • Chevalier, F.1    Chobert, J.M.2    Popineau, Y.3    Nicolas, M.G.4    Haertlé, T.5
  • 23
    • 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., Ma C.-Y. Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by Fourier transform infrared spectroscopy and differential scanning calorimetry. Journal of Agriculture and Food Chemistry 2005, 53:8046-8053.
    • (2005) Journal of Agriculture and Food Chemistry , vol.53 , pp. 8046-8053
    • Choi, S.M.1    Ma, C.-Y.2
  • 25
    • 0000352284 scopus 로고
    • Size exclusion chromatography of soybean proteins and isoflavones
    • Cole K.D., Cousin S.L. Size exclusion chromatography of soybean proteins and isoflavones. Journal of Agriculture and Food Chemistry 1994, 42:2713-2720.
    • (1994) Journal of Agriculture and Food Chemistry , vol.42 , pp. 2713-2720
    • Cole, K.D.1    Cousin, S.L.2
  • 26
    • 0002735770 scopus 로고
    • Effects of ions on protein conformation
    • American Chemical Society, Washington, DC, J. Cherry (Ed.)
    • Damodaran S., Kinsella J.E. Effects of ions on protein conformation. Food protein deterioration 1982, 301-357. American Chemical Society, Washington, DC. J. Cherry (Ed.).
    • (1982) Food protein deterioration , pp. 301-357
    • Damodaran, S.1    Kinsella, J.E.2
  • 27
    • 0030758135 scopus 로고    scopus 로고
    • Structure and thermal stability of photosystem II reaction centers studied by infrared spectroscopy
    • De Las Rivas J., Baker J. Structure and thermal stability of photosystem II reaction centers studied by infrared spectroscopy. Biochemistry 1997, 36:8897-8903.
    • (1997) Biochemistry , vol.36 , pp. 8897-8903
    • De Las Rivas, J.1    Baker, J.2
  • 28
    • 33646384737 scopus 로고    scopus 로고
    • Effects of reducing agent concentration on soy protein fractionation and functionality
    • Deak N.A., Murphy P.A., Johnson L.A. Effects of reducing agent concentration on soy protein fractionation and functionality. Journal of Food Science 2006, 71(3):C200-C208.
    • (2006) Journal of Food Science , vol.71 , Issue.3
    • Deak, N.A.1    Murphy, P.A.2    Johnson, L.A.3
  • 29
    • 33745283621 scopus 로고    scopus 로고
    • Effects of NaCl concentration on salting-in and dilution during salting-out on soy protein fractionation
    • Deak N.A., Murphy P.A., Johnson L.A. Effects of NaCl concentration on salting-in and dilution during salting-out on soy protein fractionation. Journal of Food Science 2006, 71(4):C247-C254.
    • (2006) Journal of Food Science , vol.71 , Issue.4
    • Deak, N.A.1    Murphy, P.A.2    Johnson, L.A.3
  • 32
    • 0027445113 scopus 로고
    • Protein fructosylation: Fructose and the Maillard reaction
    • Dills L.W. Protein fructosylation: Fructose and the Maillard reaction. American Journal of Clinical Nutrition 1993, 58:779S-787S.
    • (1993) American Journal of Clinical Nutrition , vol.58
    • Dills, L.W.1
  • 35
    • 84985200365 scopus 로고
    • Relationship of hydrophobicity and net charge to the solubility of milk and soy proteins
    • Hayakawa S., Nakai S. Relationship of hydrophobicity and net charge to the solubility of milk and soy proteins. Journal of Food Science 1985, 50:486-491.
    • (1985) Journal of Food Science , vol.50 , pp. 486-491
    • Hayakawa, S.1    Nakai, S.2
  • 36
    • 0026642332 scopus 로고
    • Aggregation of chymotrypsinogen: Portrait by infrared spectroscopy
    • Ismail A.A., Mantsch H.H., Wang P.T.T. Aggregation of chymotrypsinogen: Portrait by infrared spectroscopy. Biochimica et Biophysica Acta 1992, 1121:183-188.
    • (1992) Biochimica et Biophysica Acta , vol.1121 , pp. 183-188
    • Ismail, A.A.1    Mantsch, H.H.2    Wang, P.T.T.3
  • 37
    • 0019599157 scopus 로고
    • Fourier transforms in the computation of self-deconvoluted and first-order derivative spectra of overlapped band contours
    • Kauppinen J.K., Moffatt D.J., Mantsch H.H., Cameron D.G. Fourier transforms in the computation of self-deconvoluted and first-order derivative spectra of overlapped band contours. Analytical Chemistry 1981, 53:1454-1457.
    • (1981) Analytical Chemistry , vol.53 , pp. 1454-1457
    • Kauppinen, J.K.1    Moffatt, D.J.2    Mantsch, H.H.3    Cameron, D.G.4
  • 38
    • 0006994065 scopus 로고
    • Structure, surface properties and foam stability of native, reduced and succinylated soy 11 S globulins
    • Kim, S. H. (1985). Structure, surface properties and foam stability of native, reduced and succinylated soy 11 S globulins. Ph.D. Cornell University, Ithaca, NY.
    • (1985) Ph.D. Cornell University, Ithaca, NY
    • Kim, S.H.1
  • 39
    • 2342586625 scopus 로고    scopus 로고
    • Changes of glycinin conformation due to pH, heat and salt determined by differential scanning calorimetry and circular dichroism
    • Kim K.S., Kim S., Yang H.J., Kwon D.Y. Changes of glycinin conformation due to pH, heat and salt determined by differential scanning calorimetry and circular dichroism. International Journal of Food Science and Technology 2004, 39:385-393.
    • (2004) International Journal of Food Science and Technology , vol.39 , pp. 385-393
    • Kim, K.S.1    Kim, S.2    Yang, H.J.3    Kwon, D.Y.4
  • 41
    • 0000678633 scopus 로고
    • Physicochemical and functional properties of oilseed proteins with emphasis on soya proteins
    • Academic Press Inc., London, A.M. Altschul, H.L. Wilcke (Eds.)
    • Kinsella J.E., Damodaran S., German B. Physicochemical and functional properties of oilseed proteins with emphasis on soya proteins. New protein foods 1985, Academic Press Inc., London. A.M. Altschul, H.L. Wilcke (Eds.).
    • (1985) New protein foods
    • Kinsella, J.E.1    Damodaran, S.2    German, B.3
  • 43
    • 0011338066 scopus 로고
    • Purification of the 7S component of soybean proteins
    • Koshiyama I. Purification of the 7S component of soybean proteins. Agricultural and Biological Chemistry 1965, 29:885-887.
    • (1965) Agricultural and Biological Chemistry , vol.29 , pp. 885-887
    • Koshiyama, I.1
  • 44
    • 0015267271 scopus 로고
    • Purification and physicochemical properties of 11S globulin in soybean seeds
    • Koshiyama I. Purification and physicochemical properties of 11S globulin in soybean seeds. International Journal of Peptide and Protein Research 1972, 4:167-176.
    • (1972) International Journal of Peptide and Protein Research , vol.4 , pp. 167-176
    • Koshiyama, I.1
  • 45
    • 0001353395 scopus 로고
    • A heat denaturation study of the 11S globulin in soybean seeds
    • Koshiyama I. A heat denaturation study of the 11S globulin in soybean seeds. Food Chemistry 1980-1981, 6:309-322.
    • (1980) Food Chemistry , vol.6 , pp. 309-322
    • Koshiyama, I.1
  • 46
    • 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 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 49
    • 0026026725 scopus 로고
    • Divalent cation-induced changes in conformation of protein kinase C
    • Lester D.S., Brumfeld V. Divalent cation-induced changes in conformation of protein kinase C. Biophysical Chemistry 1991, 39:215-224.
    • (1991) Biophysical Chemistry , vol.39 , pp. 215-224
    • Lester, D.S.1    Brumfeld, V.2
  • 51
    • 0040815196 scopus 로고
    • Exothermic transitions of glycinin determined by differential scanning calorimetry
    • Marshall W.E., Zarins Z.M. Exothermic transitions of glycinin determined by differential scanning calorimetry. Journal of Agriculture and Food Chemistry 1989, 37:869-873.
    • (1989) Journal of Agriculture and Food Chemistry , vol.37 , pp. 869-873
    • Marshall, W.E.1    Zarins, Z.M.2
  • 53
    • 52949111347 scopus 로고    scopus 로고
    • The effect of glycation on foam and structural properties of β-lactoglobulin
    • Medrano A., Abirached C., Panizzolo L., Moyna P., Anon M.C. The effect of glycation on foam and structural properties of β-lactoglobulin. Food Chemistry 2009, 113:127-133.
    • (2009) Food Chemistry , vol.113 , pp. 127-133
    • Medrano, A.1    Abirached, C.2    Panizzolo, L.3    Moyna, P.4    Anon, M.C.5
  • 54
    • 0002448715 scopus 로고    scopus 로고
    • In: K. Liu (Ed.), Soybeans: Chemistry, technology, and utilization (1st ed.,). Chapman & Hall, NY
    • Messina, M. J. (1997). Soyfoods: Their role in disease prevention and treatment. In: K. Liu (Ed.), Soybeans: Chemistry, technology, and utilization (1st ed., pp 442-477). Chapman & Hall, NY.
    • (1997) Soyfoods: Their role in disease prevention and treatment , pp. 442-477
    • Messina, M.J.1
  • 55
    • 2642515521 scopus 로고    scopus 로고
    • Thermal properties and adhesion strength of modified soybean storage proteins
    • Mo X., Sun X., Wang D. Thermal properties and adhesion strength of modified soybean storage proteins. Journal of the American Oil Chemists' Society 2004, 81:395-400.
    • (2004) Journal of the American Oil Chemists' Society , vol.81 , pp. 395-400
    • Mo, X.1    Sun, X.2    Wang, D.3
  • 56
    • 0345059266 scopus 로고    scopus 로고
    • Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: Effect on association behavior and protein conformation
    • Morgan F., Leonil J., Molle D., Bouhallab S. Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: Effect on association behavior and protein conformation. Journal of the Agriculture and Food Chemistry 1999, 47:83-91.
    • (1999) Journal of the Agriculture and Food Chemistry , vol.47 , pp. 83-91
    • Morgan, F.1    Leonil, J.2    Molle, D.3    Bouhallab, S.4
  • 59
    • 0022245052 scopus 로고
    • The structure and complexity of the 11S polypeptides in soybeans
    • Nielsen N.C. The structure and complexity of the 11S polypeptides in soybeans. Journal of the American Oil Chemists' Society 1985, 62:1680-1686.
    • (1985) Journal of the American Oil Chemists' Society , vol.62 , pp. 1680-1686
    • Nielsen, N.C.1
  • 60
    • 0035916258 scopus 로고    scopus 로고
    • Effects of salts on the stability and folding of staphylococcal nuclease
    • Nishimura C., Uversky V.N., Fink A.L. Effects of salts on the stability and folding of staphylococcal nuclease. Biochemistry 2001, 40:2113-2128.
    • (2001) Biochemistry , vol.40 , pp. 2113-2128
    • Nishimura, C.1    Uversky, V.N.2    Fink, A.L.3
  • 62
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Evaluation of a turbidimetric technique
    • Pearce K.N., Kinsella J.E. Emulsifying properties of proteins: Evaluation of a turbidimetric technique. Journal of Agriculture and Food Chemistry 1978, 26:716-723.
    • (1978) Journal of Agriculture and Food Chemistry , vol.26 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 63
    • 0031423685 scopus 로고    scopus 로고
    • Solubility and emulsifying properties of soy protein isolates modified by pancreatin
    • Qi M., Hettiarachy N.S., Kalapathy U. Solubility and emulsifying properties of soy protein isolates modified by pancreatin. Journal of Food Science 1997, 62:1110-1115.
    • (1997) Journal of Food Science , vol.62 , pp. 1110-1115
    • Qi, M.1    Hettiarachy, N.S.2    Kalapathy, U.3
  • 64
    • 18344416037 scopus 로고    scopus 로고
    • Functional properties of improved glycinin and β-conglycinin fractions
    • Rickert D.A., Johnson L.A., Murphy P.A. Functional properties of improved glycinin and β-conglycinin fractions. Journal of Food Science 2004, 69:C303-C310.
    • (2004) Journal of Food Science , vol.69
    • Rickert, D.A.1    Johnson, L.A.2    Murphy, P.A.3
  • 65
    • 84981466858 scopus 로고
    • Differences in functional properties of 7S and 11S soybean proteins
    • Saio K., Watanabe T. Differences in functional properties of 7S and 11S soybean proteins. Journal of Texture Studies 1978, 9:135-157.
    • (1978) Journal of Texture Studies , vol.9 , pp. 135-157
    • Saio, K.1    Watanabe, T.2
  • 67
    • 0030077077 scopus 로고    scopus 로고
    • Use of sodium dodecyl sulfate polyacrylamide gel electrophoresis to measure degradation of soluble soybean proteins by Provotella ruminicola GA33 or mixed ruminal microbes in vitro
    • Schwingel W.R., Bates D.B. Use of sodium dodecyl sulfate polyacrylamide gel electrophoresis to measure degradation of soluble soybean proteins by Provotella ruminicola GA33 or mixed ruminal microbes in vitro. Journal of Animal Science 1996, 74:475-482.
    • (1996) Journal of Animal Science , vol.74 , pp. 475-482
    • Schwingel, W.R.1    Bates, D.B.2
  • 68
    • 33847797569 scopus 로고
    • Solubility profile, intrinsic viscosity, and optical rotation studies of acid precipitated soy protein and of commercial soy isolate
    • Shen J.L. Solubility profile, intrinsic viscosity, and optical rotation studies of acid precipitated soy protein and of commercial soy isolate. Journal of Agriculture and Food Chemistry 1976, 24:784-788.
    • (1976) Journal of Agriculture and Food Chemistry , vol.24 , pp. 784-788
    • Shen, J.L.1
  • 69
    • 0025874366 scopus 로고
    • Fructose induced fluorescence generation of reductively methylated glycated bovine serum albumin: Evidence for nonenzymatic glycation of Amadori products
    • Suarez G., Maturana J., Oronsky A.L., Raventos-Suarez C. Fructose induced fluorescence generation of reductively methylated glycated bovine serum albumin: Evidence for nonenzymatic glycation of Amadori products. Biochimica et Biophysica Acta 1991, 1075:12-19.
    • (1991) Biochimica et Biophysica Acta , vol.1075 , pp. 12-19
    • Suarez, G.1    Maturana, J.2    Oronsky, A.L.3    Raventos-Suarez, C.4
  • 71
    • 0021115861 scopus 로고
    • Protein structure by Fourier transform infrared spectroscopy: Second derivative spectra
    • Susi H., Byler D.M. Protein structure by Fourier transform infrared spectroscopy: Second derivative spectra. Biochemical and Biophysical Research Communications 1983, 115:391-397.
    • (1983) Biochemical and Biophysical Research Communications , vol.115 , pp. 391-397
    • Susi, H.1    Byler, D.M.2
  • 72
    • 0001984295 scopus 로고
    • Isolation and characterization of the multiple 7S globulins of soybean proteins
    • Thanh V.H., Okubo K., Shibasaki K. Isolation and characterization of the multiple 7S globulins of soybean proteins. Plant Physiology 1975, 56:19-22.
    • (1975) Plant Physiology , vol.56 , pp. 19-22
    • Thanh, V.H.1    Okubo, K.2    Shibasaki, K.3
  • 73
    • 0017019007 scopus 로고
    • Major proteins of soybean seeds: A straightforward fractionation and their characterization
    • Thanh V.H., Shibasaki K. Major proteins of soybean seeds: A straightforward fractionation and their characterization. Journal of Agriculture and Food Chemistry 1976, 24:1117-1121.
    • (1976) Journal of Agriculture and Food Chemistry , vol.24 , pp. 1117-1121
    • Thanh, V.H.1    Shibasaki, K.2
  • 74
    • 0000117038 scopus 로고
    • Relationship between hydrophobicity and foaming characteristics of food proteins
    • Townsend A., Nakai S. Relationship between hydrophobicity and foaming characteristics of food proteins. Journal of Food Science 1983, 48:588-594.
    • (1983) Journal of Food Science , vol.48 , pp. 588-594
    • Townsend, A.1    Nakai, S.2
  • 75
    • 0001129215 scopus 로고    scopus 로고
    • Thermal and electrophoretic behavior, hydrophobicity, and some functional properties of acid treated soy isolates
    • Wagner J.R., Sorgentini D.A., Anon C. Thermal and electrophoretic behavior, hydrophobicity, and some functional properties of acid treated soy isolates. Journal of Agriculture and Food Chemistry 1996, 44:1881-1889.
    • (1996) Journal of Agriculture and Food Chemistry , vol.44 , pp. 1881-1889
    • Wagner, J.R.1    Sorgentini, D.A.2    Anon, C.3
  • 76
    • 84952395389 scopus 로고
    • Foaming properties of proteins: Evaluation of a column aeration apparatus using ovalbumin
    • Waniska R.D., Kinsella J.E. Foaming properties of proteins: Evaluation of a column aeration apparatus using ovalbumin. Journal of Food Science 1979, 44:1311-1398.
    • (1979) Journal of Food Science , vol.44 , pp. 1311-1398
    • Waniska, R.D.1    Kinsella, J.E.2
  • 78
    • 0041643782 scopus 로고
    • Studies on the cold-insoluble fraction of the water-extractable soybean proteins. II. Factors influencing conformation changes in the 11S component
    • Wolf W.J., Briggs D.R. Studies on the cold-insoluble fraction of the water-extractable soybean proteins. II. Factors influencing conformation changes in the 11S component. Archives of Biochemistry and Biophysics 1958, 76:377-393.
    • (1958) Archives of Biochemistry and Biophysics , vol.76 , pp. 377-393
    • Wolf, W.J.1    Briggs, D.R.2
  • 79
    • 2842611473 scopus 로고
    • Purification and characterization of the 11S component of soybean proteins
    • Wolf W.J., Briggs D.R. Purification and characterization of the 11S component of soybean proteins. Archives of Biochemistry and Biophysics 1959, 85:186-199.
    • (1959) Archives of Biochemistry and Biophysics , vol.85 , pp. 186-199
    • Wolf, W.J.1    Briggs, D.R.2
  • 80
    • 0001544334 scopus 로고    scopus 로고
    • Partial purification and characterization of the 15S globulin of soybeans, a dimmer of glycinin
    • Wolf W.J., Nelsen T.C. Partial purification and characterization of the 15S globulin of soybeans, a dimmer of glycinin. Journal of Agriculture and Food Chemistry 1996, 44:785-791.
    • (1996) Journal of Agriculture and Food Chemistry , vol.44 , pp. 785-791
    • Wolf, W.J.1    Nelsen, T.C.2
  • 81
    • 0043152270 scopus 로고
    • Cryoprecipitation of soybean 11S protein
    • Wolf W.J., Sly D.A. Cryoprecipitation of soybean 11S protein. Cereal Chemistry 1967, 44:653-668.
    • (1967) Cereal Chemistry , vol.44 , pp. 653-668
    • Wolf, W.J.1    Sly, D.A.2
  • 85
    • 0032864734 scopus 로고    scopus 로고
    • Reactivities of d-glucose and d-fructose during glycation of bovine serum albumin
    • Yeboah F.K., Alli I., Yaylayan V.A. Reactivities of d-glucose and d-fructose during glycation of bovine serum albumin. Journal of Agriculture and Food Chemistry 1999, 47:3164-3172.
    • (1999) Journal of Agriculture and Food Chemistry , vol.47 , pp. 3164-3172
    • Yeboah, F.K.1    Alli, I.2    Yaylayan, V.A.3


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