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Volumn 21, Issue 3, 1997, Pages 255-272

Sulfhydryl and disulfide groups of the oligomeric seed globulin from amaranthus hypochondriacus K343

Author keywords

[No Author keywords available]

Indexed keywords

AMARANTHUS; AMARANTHUS CAUDATUS; AMARANTHUS HYPOCHONDRIACUS;

EID: 0031480627     PISSN: 01458884     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1745-4514.1997.tb00208.x     Document Type: Article
Times cited : (9)

References (49)
  • 2
    • 85032119438 scopus 로고
    • Determination of SH and SS-groups in some food proteins using Ellman's reagent
    • BEVERIDGE, T., TOMA, S.J. and NAKAI, S. 1974. Determination of SH and SS-groups in some food proteins using Ellman's reagent. J. Food Sci. 39, 49-51.
    • (1974) J. Food Sci. , vol.39 , pp. 49-51
    • Beveridge, T.1    Toma, S.J.2    Nakai, S.3
  • 3
    • 85004846228 scopus 로고
    • Reconstitution of conarchin from isolated subunits
    • BHUSHAN, R. and REDDING, K. 1989. Reconstitution of conarchin from isolated subunits. Int. J. Pep. Protein Res. 33, 313-316.
    • (1989) Int. J. Pep. Protein Res. , vol.33 , pp. 313-316
    • Bhushan, R.1    Redding, K.2
  • 4
    • 0001281620 scopus 로고
    • Protein fractions in amaranth grain and their chemical characterization
    • BRESSANI, B. and GARCIA-VELA, L.A. 1990. Protein fractions in amaranth grain and their chemical characterization. J. Agric. Food Chem. 38, 1205-1209.
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 1205-1209
    • Bressani, B.1    Garcia-Vela, L.A.2
  • 5
    • 84987288517 scopus 로고
    • Analysis of conformations of amino acid residues and prediction of backbone topography in proteins
    • BURGESS, A.W., PONNUSWAMY, P.K. and SCHERAGA, H.A. 1974. Analysis of conformations of amino acid residues and prediction of backbone topography in proteins. Israel J. Chem. 12, 239-286.
    • (1974) Israel J. Chem. , vol.12 , pp. 239-286
    • Burgess, A.W.1    Ponnuswamy, P.K.2    Scheraga, H.A.3
  • 6
    • 0018118041 scopus 로고
    • Circular dichroic analysis of protein conformation: Inclusion of theβ-turns
    • CHANG, C.T., WU, C.-S.C. and YANG, J.T. 1978. Circular dichroic analysis of protein conformation: Inclusion of theβ-turns. Anal. Biochem. 91, 13-31.
    • (1978) Anal. Biochem. , vol.91 , pp. 13-31
    • Chang, C.T.1    Wu, C.-S.C.2    Yang, J.T.3
  • 7
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • CHOU, P.Y. and FASMAN, G.D. 1974. Prediction of protein conformation. Biochemistry 13, 222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 8
    • 0010244985 scopus 로고
    • Human serum macroglobulins and dissociation units
    • DEUTSCH, H.F. and MORTON, J.I. 1958. Human serum macroglobulins and dissociation units. J. Biol. Chem. 231, 1107-1118.
    • (1958) J. Biol. Chem. , vol.231 , pp. 1107-1118
    • Deutsch, H.F.1    Morton, J.I.2
  • 9
    • 0039791241 scopus 로고
    • A study of factors influencing the reactivation of reduced egg white lysozyme
    • EPSTEIN, C.J. and GOLDBERGER, R.F. 1963. A study of factors influencing the reactivation of reduced egg white lysozyme. J. Biol. Chem. 238, 1380-1383.
    • (1963) J. Biol. Chem. , vol.238 , pp. 1380-1383
    • Epstein, C.J.1    Goldberger, R.F.2
  • 14
    • 0018163654 scopus 로고
    • Some characteristics of protein disulfide isomerase (E.C. 5.3.4.1) from wheat (Triticum vulgare)
    • GRYNBERG, A., NOCOLAS, J. and DRAPRON, R. 1978. Some characteristics of protein disulfide isomerase (E.C. 5.3.4.1) from wheat (Triticum vulgare). Embry. Biochemie 60, 547-551.
    • (1978) Embry. Biochemie , vol.60 , pp. 547-551
    • Grynberg, A.1    Nocolas, J.2    Drapron, R.3
  • 15
    • 0017165749 scopus 로고
    • Thiol-protein disulphide oxidoreductase: Differences between protein disulphide-isomerase and glutathione-insulin transhydrogenase activities in ox liver
    • HAWKINS, H.C. and FREEDMAN, R.B. 1976. Thiol-protein disulphide oxidoreductase: Differences between protein disulphide-isomerase and glutathione-insulin transhydrogenase activities in ox liver. Biochem. J. 159, 385-393.
    • (1976) Biochem. J. , vol.159 , pp. 385-393
    • Hawkins, H.C.1    Freedman, R.B.2
  • 16
    • 84985200365 scopus 로고
    • Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins
    • HAYAKAWA, S. and NAKAI, S. 1985. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. J. Food Sci. 50, 486-491.
    • (1985) J. Food Sci. , vol.50 , pp. 486-491
    • Hayakawa, S.1    Nakai, S.2
  • 17
    • 0019871893 scopus 로고
    • Information content in the circular dichroism of proteins
    • HENNESSEY, JR., J.P. and JOHNSON, JR., W.C. 1981. Information content in the circular dichroism of proteins. Biochemistry 20, 1085-1094.
    • (1981) Biochemistry , vol.20 , pp. 1085-1094
    • Hennessey J.P., Jr.1    Johnson W.C., Jr.2
  • 18
    • 0013341664 scopus 로고
    • Identification and purification of a purothionin homologue from rye (Secale cereale L.)
    • HERNANDEZ-LUCAS, C., CARBONERO, P. and GARCIA-OLMEDO, F. 1978. Identification and purification of a purothionin homologue from rye (Secale cereale L.). J. Agric. Food Chem. 26, 794-796.
    • (1978) J. Agric. Food Chem. , vol.26 , pp. 794-796
    • Hernandez-Lucas, C.1    Carbonero, P.2    Garcia-Olmedo, F.3
  • 19
    • 0017144476 scopus 로고
    • Thiol-protein disulphide oxidoreductase: Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase
    • IBBETSON, A.L. and FREEDMAN, R.B. 1976. Thiol-protein disulphide oxidoreductase: Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase. Biochem. J. 159, 337-384.
    • (1976) Biochem. J. , vol.159 , pp. 337-384
    • Ibbetson, A.L.1    Freedman, R.B.2
  • 20
    • 0015935066 scopus 로고
    • Direct spectrophotometric measurement of the rate of reduction of disulfide bonds
    • IYER, K.S. and KLELE, W.A. 1973. Direct spectrophotometric measurement of the rate of reduction of disulfide bonds. J. Biol. Chem. 25, 707-710.
    • (1973) J. Biol. Chem. , vol.25 , pp. 707-710
    • Iyer, K.S.1    Klele, W.A.2
  • 21
    • 0001015635 scopus 로고
    • Reduction of purothionin by the wheat seed thioredoxin system
    • JOHNSON, T.C., WADA, K., BUCHANAN, B.B. and HOLMGREN, A. 1987. Reduction of purothionin by the wheat seed thioredoxin system. Plant Physiol. 85, 446-451.
    • (1987) Plant Physiol. , vol.85 , pp. 446-451
    • Johnson, T.C.1    Wada, K.2    Buchanan, B.B.3    Holmgren, A.4
  • 22
    • 0002207547 scopus 로고
    • Relationship between structure and functional properties of food proteins
    • P.F. Fox and J.S. Condon, eds. Applied Science Publishers, New York
    • KINSELLA, J.E. 1982. Relationship between structure and functional properties of food proteins. In Food Proteins, (P.F. Fox and J.S. Condon, eds.) pp. 51-103, Applied Science Publishers, New York.
    • (1982) Food Proteins , pp. 51-103
    • Kinsella, J.E.1
  • 23
    • 0014799289 scopus 로고
    • Reversible polymerization of histidine ammonium lyase
    • KLEE, C.B. 1970. Reversible polymerization of histidine ammonium lyase. J. Biol. Chem. 245, 3143-3152.
    • (1970) J. Biol. Chem. , vol.245 , pp. 3143-3152
    • Klee, C.B.1
  • 24
    • 0040383452 scopus 로고
    • Thetin-homocysteine methylpherase: A study in molecular organization
    • S.K. Shapiro and F. Schlenk, eds. University of Chicago Press, Chicago, IL
    • KLEE, W.A. 1965. Thetin-homocysteine methylpherase: a study in molecular organization. In Transmethylation and Methionine Biosynthesis, (S.K. Shapiro and F. Schlenk, eds.) pp. 220-230, University of Chicago Press, Chicago, IL.
    • (1965) Transmethylation and Methionine Biosynthesis , pp. 220-230
    • Klee, W.A.1
  • 25
    • 84954909864 scopus 로고
    • Extraction of two albumin fractions from amaranth grains: Comparison of some physiochemical properties and putative localization in the grains
    • KONISHI, Y., HORIKAWA, K., OKU, Y., AZUMAYA, J. and NAKATANI, N. 1991. Extraction of two albumin fractions from amaranth grains: Comparison of some physiochemical properties and putative localization in the grains. Agric. Biol. Chem. 55(11), 2745-2750.
    • (1991) Agric. Biol. Chem. , vol.55 , Issue.11 , pp. 2745-2750
    • Konishi, Y.1    Horikawa, K.2    Oku, Y.3    Azumaya, J.4    Nakatani, N.5
  • 26
    • 0000452895 scopus 로고
    • Amaranth globulin as a heat-stable emulsifying agent
    • KONISHI, Y. and YOSHIMOTO, N. 1989. Amaranth globulin as a heat-stable emulsifying agent. Agric. Biol. Chem. 53(12), 3327-3328.
    • (1989) Agric. Biol. Chem. , vol.53 , Issue.12 , pp. 3327-3328
    • Konishi, Y.1    Yoshimoto, N.2
  • 27
    • 0020787176 scopus 로고
    • Structural properties of homogenous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure
    • LAMBERT, N. and FREEDMAN, R.B. 1983. Structural properties of homogenous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure. Biochem. J. 213, 225-234.
    • (1983) Biochem. J. , vol.213 , pp. 225-234
    • Lambert, N.1    Freedman, R.B.2
  • 28
    • 0000430245 scopus 로고
    • Reactivation and hybridization of reduced alkaline phosphatase
    • LEVINTHAL, C., SIGNER, E.R. and FETHEROLF, K. 1963. Reactivation and hybridization of reduced alkaline phosphatase. Proc. Nat. Acad. Sci. USA 48, 1230-1237.
    • (1963) Proc. Nat. Acad. Sci. USA , vol.48 , pp. 1230-1237
    • Levinthal, C.1    Signer, E.R.2    Fetherolf, K.3
  • 29
    • 0028065111 scopus 로고
    • Purification and characterization of the physicochemical properties of the albumin fraction of Amaranthus hypochondriacus
    • MARCONE, M.F., NIEKAMP, F.K., LE MAGUER, M. and YADA, R.Y. 1994. Purification and characterization of the physicochemical properties of the albumin fraction of Amaranthus hypochondriacus. Food Chem. 51, 287-294.
    • (1994) Food Chem. , vol.51 , pp. 287-294
    • Marcone, M.F.1    Niekamp, F.K.2    Le Maguer, M.3    Yada, R.Y.4
  • 30
    • 0000694536 scopus 로고
    • Isolation, purification and characterization of the oligomeric seed globulin from Amaranthus hypochondriacus
    • MARCONE, M.F. and YADA, R.Y. 1991. Isolation, purification and characterization of the oligomeric seed globulin from Amaranthus hypochondriacus. Agric. Biol. Chem. 55(9), 2281-2289.
    • (1991) Agric. Biol. Chem. , vol.55 , Issue.9 , pp. 2281-2289
    • Marcone, M.F.1    Yada, R.Y.2
  • 31
    • 0000253701 scopus 로고
    • Study of the charge profile and covalent subunit association of oligomeric seed globulin from Amaranthus hypochondriacus
    • MARCONE, M.F. and YADA, R.Y. 1992. Study of the charge profile and covalent subunit association of oligomeric seed globulin from Amaranthus hypochondriacus. J. Agric. Food Chem. 40(3), 385-389.
    • (1992) J. Agric. Food Chem. , vol.40 , Issue.3 , pp. 385-389
    • Marcone, M.F.1    Yada, R.Y.2
  • 32
    • 0029111306 scopus 로고
    • Isolation, purification and characterization of the seed storage globulin and its polymerized form from Triticum aestivum
    • MARCONE, M.F. and YADA, R.Y. 1995. Isolation, purification and characterization of the seed storage globulin and its polymerized form from Triticum aestivum. J. Food Biochem. 18, 123-145.
    • (1995) J. Food Biochem. , vol.18 , pp. 123-145
    • Marcone, M.F.1    Yada, R.Y.2
  • 34
    • 0014865003 scopus 로고
    • Reduction and reoxidation of pepsinogen and pepsin
    • NAKAGAWA, Y. and PERLMANN, G.E. 1970. Reduction and reoxidation of pepsinogen and pepsin. Arch. Biochem. Biophys. 140, 464-473.
    • (1970) Arch. Biochem. Biophys. , vol.140 , pp. 464-473
    • Nakagawa, Y.1    Perlmann, G.E.2
  • 35
    • 0000454769 scopus 로고
    • Denaturation of soybean proteins by isoelectric precipitation
    • NASH, A.M., KWALEK, W.F. and WOLF, W.J. 1971. Denaturation of soybean proteins by isoelectric precipitation. Cereal Chem. 48, 360-368.
    • (1971) Cereal Chem. , vol.48 , pp. 360-368
    • Nash, A.M.1    Kwalek, W.F.2    Wolf, W.J.3
  • 36
    • 0040977672 scopus 로고
    • 50 01 255 P100, Pharmacia LKB, S-75182 Uppsala, Sweden
    • Pharmacia LKB. 1985. Separation Technique File No. 100, (50 01 255 P100), Pharmacia LKB, S-75182 Uppsala, Sweden.
    • (1985) Separation Technique File , vol.100
  • 37
    • 84982366332 scopus 로고
    • Reduction and re-oxidation of the purothionins
    • REDMAN, D.G. and ELTON, G.A. 1969. Reduction and re-oxidation of the purothionins. J. Sci. Food Agric. 20, 546-549.
    • (1969) J. Sci. Food Agric. , vol.20 , pp. 546-549
    • Redman, D.G.1    Elton, G.A.2
  • 38
    • 84982361752 scopus 로고
    • Purothionin analoques from barley flour
    • REDMAN, R.C. and FISHER, N. 1969. Purothionin analoques from barley flour. J. Sci. Food Agric. 20, 427-432.
    • (1969) J. Sci. Food Agric. , vol.20 , pp. 427-432
    • Redman, R.C.1    Fisher, N.2
  • 39
    • 0000309081 scopus 로고
    • Protein disulphide-isomerase is located in the endoplasmic reticulum of developing wheat endosperm
    • RODEN, L.T., MIFLIN, B.J. and FREEDMAN, R.B. 1982. Protein disulphide-isomerase is located in the endoplasmic reticulum of developing wheat endosperm. FEBS Lett. 138, 121-124.
    • (1982) FEBS Lett. , vol.138 , pp. 121-124
    • Roden, L.T.1    Miflin, B.J.2    Freedman, R.B.3
  • 40
    • 0004153150 scopus 로고
    • The covalent structure of proteins
    • G.E. Schulz and R.H. Schirmer, eds. Springer-Verlag, New York
    • SCHULTZ, G.E. and SCHIRMER, R.H. 1979. The Covalent Structure of Proteins. In Principles of Protein Structure, 2nd Ed., (G.E. Schulz and R.H. Schirmer, eds.) pp. 46-65, Springer-Verlag, New York.
    • (1979) Principles of Protein Structure, 2nd Ed. , pp. 46-65
    • Schultz, G.E.1    Schirmer, R.H.2
  • 41
    • 0013838236 scopus 로고
    • Enzymically catalyzed disulfide interchange in randomly cross-linked soybean trypsin inhibitor
    • STEINER, R.F. 1965. Enzymically catalyzed disulfide interchange in randomly cross-linked soybean trypsin inhibitor. J. Biol. Chem. 240, 4648-4651.
    • (1965) J. Biol. Chem. , vol.240 , pp. 4648-4651
    • Steiner, R.F.1
  • 42
    • 84912633113 scopus 로고
    • D. Metzler, ed. Pergamon Press, Oxford, England
    • TORCHINSKII, YU. M. 1981. Sulfur in Proteins (D. Metzler, ed.) pp. 1-311, Pergamon Press, Oxford, England.
    • (1981) Sulfur in Proteins , pp. 1-311
    • Torchinskii, Y.U.M.1
  • 43
    • 0040383449 scopus 로고
    • Purothionin: A seed protein with thioredozin activity
    • Tokyo
    • WADA, K. and BUCHANAN, B.B. 1981. Purothionin: A seed protein with thioredozin activity. J. Biochem. (Tokyo) 124(2), 237-240.
    • (1981) J. Biochem. , vol.124 , Issue.2 , pp. 237-240
    • Wada, K.1    Buchanan, B.B.2
  • 44
    • 0001707594 scopus 로고
    • Sulfhydryl content of glycinin: Effect of reducing agents
    • WOLF, W.J. 1993. Sulfhydryl content of glycinin: Effect of reducing agents. J. Agric. Food Chem. 41, 168-176.
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 168-176
    • Wolf, W.J.1
  • 45
    • 0010773959 scopus 로고
    • Behavior of the 11S protein of soybeans in acid solutions. I. Effects of pH, ionic strength and time on ultracentrifugal and optical rotatory properties
    • WOLF, W.J., RACKIS, J.J., SMITH, A.K., SASAME, H.A. and BABCOCK, G.E. 1958. Behavior of the 11S protein of soybeans in acid solutions. I. Effects of pH, ionic strength and time on ultracentrifugal and optical rotatory properties. J. Am. Chem. Soc. 80, 5730-5735.
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 5730-5735
    • Wolf, W.J.1    Rackis, J.J.2    Smith, A.K.3    Sasame, H.A.4    Babcock, G.E.5
  • 46
    • 0001647758 scopus 로고
    • Electrophoretical and differential thermal analysis of soybean 11S globulin heated in the presence of N-ethylmaleimide
    • YAMAGISHI, T., YAMAUCHI, F. and SHIBASAKI, K. 1981. Electrophoretical and differential thermal analysis of soybean 11S globulin heated in the presence of N-ethylmaleimide. Agric. Biol. Chem. 45(7), 1661-1668.
    • (1981) Agric. Biol. Chem. , vol.45 , Issue.7 , pp. 1661-1668
    • Yamagishi, T.1    Yamauchi, F.2    Shibasaki, K.3
  • 47
    • 0017804559 scopus 로고
    • Fluorescent tracer methods for protein SH groups. II
    • YAMAMOTO, K., OKAMOTO, Y. and SEKINE, T. 1978. Fluorescent tracer methods for protein SH groups. II. Anal. Biochem. 84, 313-318.
    • (1978) Anal. Biochem. , vol.84 , pp. 313-318
    • Yamamoto, K.1    Okamoto, Y.2    Sekine, T.3
  • 49
    • 0014339244 scopus 로고
    • The mechanism of refolding of the reduced random coil form of lysozyme
    • YUTANI, K., YUTANI, A., IMANISHI, A. and ISEMURA, T. 1968. The mechanism of refolding of the reduced random coil form of lysozyme. J. Biochem. 64, 449-455.
    • (1968) J. Biochem. , vol.64 , pp. 449-455
    • Yutani, K.1    Yutani, A.2    Imanishi, A.3    Isemura, T.4


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