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Volumn 46, Issue 6, 1998, Pages 2080-2086

Structural Changes of Legumin from Faba Beans (Vicia faba L.) by Succinylation

Author keywords

Conformational changes; Faba bean protein; Legumin; Succinylation

Indexed keywords

PHASEOLUS (ANGIOSPERM); VICIA FABA;

EID: 0001506074     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf970984k     Document Type: Article
Times cited : (24)

References (38)
  • 1
    • 0023056522 scopus 로고
    • The legumin gene family: Structure of a B type gene of Vicia faba and a possible legumin gene specific regulatory element
    • Bäumlein, H.; Wobus, U.; Pustell, J.; Kafatos, F. C. The legumin gene family: structure of a B type gene of Vicia faba and a possible legumin gene specific regulatory element. Nucleic Acids Res. 1986, 14, 2707-2720.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 2707-2720
    • Bäumlein, H.1    Wobus, U.2    Pustell, J.3    Kafatos, F.C.4
  • 2
    • 0017836185 scopus 로고
    • Structural studies on the succinylated bovine serum albumin
    • Chang, T.-S.; Sun, S. F. Structural studies on the succinylated bovine serum albumin. Int. J. Peptide Protein Res. 1978, 11, 65-72.
    • (1978) Int. J. Peptide Protein Res. , vol.11 , pp. 65-72
    • Chang, T.-S.1    Sun, S.F.2
  • 4
    • 0028511883 scopus 로고
    • Proteins at liquid interfaces: Role of the molten globule state
    • Dickinson, E.; Matsumura, Y. Proteins at liquid interfaces: role of the molten globule state. Colloids Surf. B: Biointerfaces 1994, 3, 1-17.
    • (1994) Colloids Surf. B: Biointerfaces , vol.3 , pp. 1-17
    • Dickinson, E.1    Matsumura, Y.2
  • 5
    • 0006460027 scopus 로고    scopus 로고
    • Limited tryptic hydrolysis of legumin from faba bean (Vicia faba L.): Formation of an unequal subunit pattern
    • Dudek, S.; Horstmann, C.; Schwenke, K. D. Limited tryptic hydrolysis of legumin from faba bean (Vicia faba L.): formation of an unequal subunit pattern. Nahrung 1996, 40, 171-176.
    • (1996) Nahrung , vol.40 , pp. 171-176
    • Dudek, S.1    Horstmann, C.2    Schwenke, K.D.3
  • 6
    • 77957004481 scopus 로고
    • The rapid determination of amino groups with TNBS
    • Fields, R. The rapid determination of amino groups with TNBS. Methods Enzymol. 1972, 25B, 464-468.
    • (1972) Methods Enzymol. , vol.25 B , pp. 464-468
    • Fields, R.1
  • 7
    • 0041341327 scopus 로고
    • Functional properties of succinylated and acetylated soy protein
    • Franzen, K. L.; Kinsella, J. E.Functional properties of succinylated and acetylated soy protein. J. Agric. Food Chem. 1976, 24, 788-795.
    • (1976) J. Agric. Food Chem. , vol.24 , pp. 788-795
    • Franzen, K.L.1    Kinsella, J.E.2
  • 8
    • 0014198584 scopus 로고
    • Succinylation of pepsinogen
    • Gounaris, A. D.; Perlman, G. E. Succinylation of pepsinogen. J. Biol. Chem. 1967, 242, 2739-2745.
    • (1967) J. Biol. Chem. , vol.242 , pp. 2739-2745
    • Gounaris, A.D.1    Perlman, G.E.2
  • 9
    • 0002552293 scopus 로고
    • Effect of succinylation on some physicochemical and functional properties of the 12 S storage protein from rapeseed (Brassica napus L.)
    • Gueguen, J.; Bollecker, S.; Schwenke, K. D.; Raab, B. Effect of succinylation on some physicochemical and functional properties of the 12 S storage protein from rapeseed (Brassica napus L.). J. Agric. Food Chem. 1990, 38, 61-69.
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 61-69
    • Gueguen, J.1    Bollecker, S.2    Schwenke, K.D.3    Raab, B.4
  • 10
    • 0014546290 scopus 로고
    • Enzymic and immunochemical properties of lysozyme II. Conformation, immunochemistry and enzymic activity of a derivative modified at tryptophan
    • Habeeb, A. F. S. A.; Atassi, M. Z. Enzymic and immunochemical properties of lysozyme II. Conformation, immunochemistry and enzymic activity of a derivative modified at tryptophan. Immunochemistry 1969, 6, 555-566.
    • (1969) Immunochemistry , vol.6 , pp. 555-566
    • Habeeb, A.F.S.A.1    Atassi, M.Z.2
  • 11
    • 50549198780 scopus 로고
    • A micro-biuret method for estimating proteins
    • Itzhaki, R. F.; Gill, D. M. A micro-biuret method for estimating proteins. Anal. Biochem. 1964, 9, 401-410.
    • (1964) Anal. Biochem. , vol.9 , pp. 401-410
    • Itzhaki, R.F.1    Gill, D.M.2
  • 12
    • 0014961145 scopus 로고
    • Partial modification of bovine serum albumin with dicarboxylic anhydrides. Physical properties of the modified species
    • Jonas, A.; Weber, G. Partial modification of bovine serum albumin with dicarboxylic anhydrides. Physical properties of the modified species. Biochemistry 1970, 9, 4729-4735.
    • (1970) Biochemistry , vol.9 , pp. 4729-4735
    • Jonas, A.1    Weber, G.2
  • 13
    • 84991180393 scopus 로고
    • Functional properties of acetylated and succinylated sunflower protein isolate
    • Kabirullah, M.; Wills, R. B. H. Functional properties of acetylated and succinylated sunflower protein isolate. J. Food Technol. 1982, 17, 235-249.
    • (1982) J. Food Technol. , vol.17 , pp. 235-249
    • Kabirullah, M.1    Wills, R.B.H.2
  • 14
    • 0019331914 scopus 로고
    • Hydrophobicity determinated by a fiuorescence probe method and its correlation with surface properties of proteins
    • Kato, A.; Nakai, S. Hydrophobicity determinated by a fiuorescence probe method and its correlation with surface properties of proteins. Biochim. Biophys. Acta 1980, 624, 13-20.
    • (1980) Biochim. Biophys. Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 15
    • 0000525996 scopus 로고
    • Effect of progressive succinylation on some molecular properties of soy glycinin
    • Kim, S. H.; Kinsella, I. E. Effect of progressive succinylation on some molecular properties of soy glycinin. Cereal Chem. 1986, 63, 342-345.
    • (1986) Cereal Chem. , vol.63 , pp. 342-345
    • Kim, S.H.1    Kinsella, I.E.2
  • 16
    • 0001589422 scopus 로고    scopus 로고
    • Some physicochemical and interfacial properties of native and acetylated legumin from faba beans (Vicia faba L.)
    • Krause, J.-P.; Mothes, R.; Schwenke, K. D. Some physicochemical and interfacial properties of native and acetylated legumin from faba beans (Vicia faba L.). J. Agric. Food Chem. 1996, 44, 429-437.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 429-437
    • Krause, J.-P.1    Mothes, R.2    Schwenke, K.D.3
  • 17
    • 0343907243 scopus 로고    scopus 로고
    • Properties of intercial films formed by succinylated legumin from faba beans (Vicia faba L.)
    • Krause, J.-P.; Krägel, J.; Schwenke, K. D. Properties of intercial films formed by succinylated legumin from faba beans (Vicia faba L.). Colloids Surf. B: Biointerfaces 1997, 8, 279-286.
    • (1997) Colloids Surf. B: Biointerfaces , vol.8 , pp. 279-286
    • Krause, J.-P.1    Krägel, J.2    Schwenke, K.D.3
  • 18
    • 0026864191 scopus 로고
    • Kinetics of adsorption of globular proteins at an air-water interface
    • Narsimhan, G.; Uraizee, F. Kinetics of adsorption of globular proteins at an air-water interface.Biotechnol. Progr. 1992, 8, 187-196.
    • (1992) Biotechnol. Progr. , vol.8 , pp. 187-196
    • Narsimhan, G.1    Uraizee, F.2
  • 19
    • 0039427658 scopus 로고
    • Rheologiy and microstructure of succinylated canola protein isolate
    • Paulson, A. T.; Tung, M. A. Rheologiy and microstructure of succinylated canola protein isolate. J. Food Sci. 1988, 53, 821-825.
    • (1988) J. Food Sci. , vol.53 , pp. 821-825
    • Paulson, A.T.1    Tung, M.A.2
  • 20
    • 0020709925 scopus 로고
    • The structure of 11 S globulins from sunflower and rape seed a small-angle X-ray scattering study
    • Plietz, P.; Damaschun, G.; Müller, J. J.; Schwenke, K. D. The structure of 11 S globulins from sunflower and rape seed a small-angle X-ray scattering study. Eur. J. Biochem. 1983, 130, 315-320.
    • (1983) Eur. J. Biochem. , vol.130 , pp. 315-320
    • Plietz, P.1    Damaschun, G.2    Müller, J.J.3    Schwenke, K.D.4
  • 21
    • 0001162505 scopus 로고
    • Relationship between the amino acid sequence and the domain structure of the subunits of the 11 S seed globulins
    • Plietz, P.; Drescher, B.; Damaschun, G.Relationship between the amino acid sequence and the domain structure of the subunits of the 11 S seed globulins. Int. J. Biol. Macromol. 1987, 9, 161-165.
    • (1987) Int. J. Biol. Macromol. , vol.9 , pp. 161-165
    • Plietz, P.1    Drescher, B.2    Damaschun, G.3
  • 22
    • 0001962772 scopus 로고
    • Isolation and purification of 11 S globulins from seeds of broad beans and peas
    • in Russian
    • Popello, I. A.; Suchkov, V. V.; Grinberg, V. Y.; Tolstoguzov, V. B. Isolation and purification of 11 S globulins from seeds of broad beans and peas. Prikl. Biochem. Mikrobiol. 1988, 24, 50-55 (in Russian).
    • (1988) Prikl. Biochem. Mikrobiol. , vol.24 , pp. 50-55
    • Popello, I.A.1    Suchkov, V.V.2    Grinberg, V.Y.3    Tolstoguzov, V.B.4
  • 23
    • 0002940127 scopus 로고
    • The molten globule state
    • Creighton, T. E., Ed.; Freeman: New York
    • Ptitsyn, O. B. The molten globule state. In Protein Folding; Creighton, T. E., Ed.; Freeman: New York, 1992; pp 243-300.
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 24
    • 0021759419 scopus 로고
    • Determination of tyrosine exposure in proteins by second-derivative spectroscopy
    • Ragone, R.; Colonna, G.; Balestrieri, C.; Servillo, L.; Irace, G. Determination of tyrosine exposure in proteins by second-derivative spectroscopy. Biochemistry 1984, 23, 1871-1875.
    • (1984) Biochemistry , vol.23 , pp. 1871-1875
    • Ragone, R.1    Colonna, G.2    Balestrieri, C.3    Servillo, L.4    Irace, G.5
  • 25
    • 0018526460 scopus 로고
    • Effect of succinylation on the oligomeric structure of glycinin
    • Rao, A. G. A.; Rao, M. S. N. Effect of succinylation on the oligomeric structure of glycinin. Int. J. Pept. Protein Res. 1979, 14, 307-312.
    • (1979) Int. J. Pept. Protein Res. , vol.14 , pp. 307-312
    • Rao, A.G.A.1    Rao, M.S.N.2
  • 26
    • 84984508941 scopus 로고
    • Chemische Modifizierung von Proteinen. 8. Mitt. Beeinflussung physikochemischer und funktioneller Eigenschaften von Proteinen aus Ackerbohnen durch Succinylierung
    • Rauschal, E. J.; Linow, K.-J.; Pähtz, W.; Schwenke, K. D. Chemische Modifizierung von Proteinen. 8. Mitt. Beeinflussung physikochemischer und funktioneller Eigenschaften von Proteinen aus Ackerbohnen durch Succinylierung (Chemical modification of proteins. Part 8. Effect of succinylation on physicochemical and functional properties of proteins from faba beans). Nahrung 1981, 25, 241-248.
    • (1981) Nahrung , vol.25 , pp. 241-248
    • Rauschal, E.J.1    Linow, K.-J.2    Pähtz, W.3    Schwenke, K.D.4
  • 27
    • 0000413242 scopus 로고
    • Succinylcarboxypeptidase
    • Riordan, J. F.; Vallee, B. L. Succinylcarboxypeptidase. Biochemistry 1964, 3, 1768-1774.
    • (1964) Biochemistry , vol.3 , pp. 1768-1774
    • Riordan, J.F.1    Vallee, B.L.2
  • 28
    • 0025649275 scopus 로고
    • The cDNA derived primary structure of two distinct legumin A subunit precursors from field bean (Vicia faba L.)
    • Schlesier, B.; Bassüner, R.; Van Hai, N.; Müntz, K. The cDNA derived primary structure of two distinct legumin A subunit precursors from field bean (Vicia faba L.). Nucleic Acids Res. 1990, 18, 7146.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 7146
    • Schlesier, B.1    Bassüner, R.2    Van Hai, N.3    Müntz, K.4
  • 29
    • 85004870426 scopus 로고
    • Structural changes of the 11 S globulin from sunflower seed (Helianthus annuus L.) after succinylation
    • Schwenke, K. D.; Rauschal, E.; Zirwer, D.; Linow, K.-J. Structural changes of the 11 S globulin from sunflower seed (Helianthus annuus L.) after succinylation. Int. J. Pept. Protein Res. 1985, 25, 347-354.
    • (1985) Int. J. Pept. Protein Res. , vol.25 , pp. 347-354
    • Schwenke, K.D.1    Rauschal, E.2    Zirwer, D.3    Linow, K.-J.4
  • 30
    • 84982585010 scopus 로고
    • Modification of the oligomeric structure of 11 S globulin from sunflower (Helianthus annuus L.) and rape (Brassica napus L.) seeds by succinylation
    • Schwenke, K. D.; Linow, K.-J.; Zirwer, D. Modification of the oligomeric structure of 11 S globulin from sunflower (Helianthus annuus L.) and rape (Brassica napus L.) seeds by succinylation. Nahrung 1986, 30, 263-270.
    • (1986) Nahrung , vol.30 , pp. 263-270
    • Schwenke, K.D.1    Linow, K.-J.2    Zirwer, D.3
  • 31
    • 0025671945 scopus 로고
    • Changes of the oligomeric structure of legumin from pea (Pisum sativum L.) after succinylation
    • Schwenke, K. D.; Zirwer, D.; Gast, K.; Görnitz, E.; Linow, K.-J.; Gueguen, J. Changes of the oligomeric structure of legumin from pea (Pisum sativum L.) after succinylation. Eur. J. Biochem. 1990, 194, 621-627.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 621-627
    • Schwenke, K.D.1    Zirwer, D.2    Gast, K.3    Görnitz, E.4    Linow, K.-J.5    Gueguen, J.6
  • 32
    • 0038395173 scopus 로고
    • Dissociation of 11 S globulins from plant seeds after succinylation - A problem of subunit interaction
    • Visser, H., Ed.; VCH: Weinheim
    • Schwenke, K. D.; Zirwer, D.; Gast, K.; Linow, K.-J.; Görnitz, E.; Gueguen, J.; Subirade, M. Dissociation of 11 S globulins from plant seeds after succinylation - a problem of subunit interaction. In Protein Interactions; Visser, H., Ed.; VCH: Weinheim 1992; pp 233-252.
    • (1992) Protein Interactions , pp. 233-252
    • Schwenke, K.D.1    Zirwer, D.2    Gast, K.3    Linow, K.-J.4    Görnitz, E.5    Gueguen, J.6    Subirade, M.7
  • 33
    • 84984499625 scopus 로고
    • Physicochemical and enzymatic studies on acetylated protein isolates from faba beans (Vicia faba L.)
    • Schwenke, K. D.; Dudek, S.; Mothes, R.; Raab, B.; Seifert, A. Physicochemical and enzymatic studies on acetylated protein isolates from faba beans (Vicia faba L.). Nahrung 1993, 37, 258-268.
    • (1993) Nahrung , vol.37 , pp. 258-268
    • Schwenke, K.D.1    Dudek, S.2    Mothes, R.3    Raab, B.4    Seifert, A.5
  • 34
    • 84984450310 scopus 로고
    • Isolation of faba bean legumin - A comparative study of various methods
    • Schwenke, K. D.; Dudek, S.; Seifert, A.; Mothes, R.; Staate, A. Isolation of faba bean legumin - a comparative study of various methods. Nahrung 1994, 38, 557-567.
    • (1994) Nahrung , vol.38 , pp. 557-567
    • Schwenke, K.D.1    Dudek, S.2    Seifert, A.3    Mothes, R.4    Staate, A.5
  • 35
    • 84984423730 scopus 로고
    • Legumin-T from faba bean legumin: Isolation, partial characterization and surface functional properties
    • Schwenke, K. D.; Staatz, A.; Dudek, S.; Krause, J.-P.; Noack, J. Legumin-T from faba bean legumin: isolation, partial characterization and surface functional properties. Nahrung 1995, 39, 193-202.
    • (1995) Nahrung , vol.39 , pp. 193-202
    • Schwenke, K.D.1    Staatz, A.2    Dudek, S.3    Krause, J.-P.4    Noack, J.5
  • 36
    • 0542406967 scopus 로고
    • Improved approach for characterizing the coalescence stability of legumin stabilzed O/W emulsions by analytical ultracentrifugation
    • Seifert, A.; Schwenke, K. D. Improved approach for characterizing the coalescence stability of legumin stabilzed O/W emulsions by analytical ultracentrifugation. Prog. Colloid Polym. Sci. 1995, 31, 38.
    • (1995) Prog. Colloid Polym. Sci. , vol.31 , pp. 38
    • Seifert, A.1    Schwenke, K.D.2
  • 37
    • 0017888209 scopus 로고
    • Effect of succinylation on the oligomeric structure of arachin
    • Shetty, K. Y.; Rao, M. S. N. Effect of succinylation on the oligomeric structure of arachin. Int. J. Pept. Protein Res. 1978, 11, 305-313.
    • (1978) Int. J. Pept. Protein Res. , vol.11 , pp. 305-313
    • Shetty, K.Y.1    Rao, M.S.N.2
  • 38
    • 0000467495 scopus 로고
    • Effect of dissociation and conformational changes on the surface behavior of pea legumin
    • Subirade, M.; Gueguen, J.; Schwenke, K. D. Effect of dissociation and conformational changes on the surface behavior of pea legumin. J. Colloid Interface Sci. 1992, 152, 442-454.
    • (1992) J. Colloid Interface Sci. , vol.152 , pp. 442-454
    • Subirade, M.1    Gueguen, J.2    Schwenke, K.D.3


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