Shape, symmetry, hydration and secondary structure of the legumin from Vicia faba in solution

Plietz, P.; Zirwer, Dietrich; Schlesier, Bernhard; Gast, Klaus; Damaschun, G.

doi:10.1016/0167-4838(84)90120-1

Cited by 63 publications

(33 citation statements)

References 15 publications

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“…Molar mass estimation using protein standards yielded (250 11) kDa for legumin-T, while the native legumin gave (345 f 15) kDa. Both data corresponds well with the values determined by PLIETZ et al [27] for native legumin, and by our laboratory for legumin-T [28] using hydrodynamic methods and static light scattering. The value found for legumin-T is, however, significantly lower than that determined by DANILENKO and colleagues [7 -…”

Section: Gelchromatographic Analysissupporting

confidence: 71%

“…The quaternary structure of native legumin is characterized by an arrangement of six subunits [27] having a molecular mass of 55 -60 kDa [34]. In contrast to that, the legumin-T preparation described in the present paper shows an "unequal" subunit pattern.…”

Section: Discussionmentioning

confidence: 80%

“…1 where k is the Boltzman-constant and qo is the viscosity of the solvent (q,, = 1.062 cP). Using R, = 5.55 nm we obtained Dapp = 3.7 1 x lo-' cm's -I , whereas a value of D20,w = 3.38 x lo-' cm2 sC1 was reported for native legumin [27].…”

Section: Discussionmentioning

confidence: 90%

“…Both are slightly higher than the corresponding values obtained by hydrodynamic methods. The latter gave (5.0 f 0,09) nm for legumin-T [28], and (6.32 & 0.15) for legumin [27]. Gel electrophoretic studies Fig.…”

Section: Gelchromatographic Analysismentioning

confidence: 97%

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Legumin‐T from faba bean legumin: Isolation, partial characterization and surface functional properties

Schwenke

Staatz

Dudek

et al. 1995

Nahrung

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SummaryLegumin-T was prepared by limited tryptic hydrolysis of legumin from faba beans (Viciu faba L.) and was chromatographically purified. It is composed of two principle subunits consisting each of an intact P-polypeptide chain and a nicked a-chain of legumin besides minor polypeptides. The molecular mass was (250 f 11) kDa estimated by gel chromatography. Amino acid analysis showed that the transformation of legumin to legumin-T resulted in a loss of polar amino acids and an increase of non-polar hydrophobic amino acids. The time-dependent surface tension and the surface compressions isotherms showed a rather similar behavior of legumin and legumin-T. The calculated ratio of the surface areas A / A o revealed, however, difference between both proteins (legumin: A / A , = 1, legurnin-T: A / A o < 1) pointing to an irreversible desorption of legumin-T from the surface due to compression. The emulsifying activity of legumin-T was higher than that of the parent legumin. ZusamrnenfassungLegumin-T aus Ackerbohnen: Isolierung, teilweise Charakterisierung und Grenzflachenfunktionalitlt Legurnin-T wurde durch begrenzte tryptische Hydrolyse von Legumin aus Ackerbohnen (Viciafaba L.) gewonnen und gelchromatographisch gereinigt. Es besteht aus zwei verschiedenen UntereinheitenTypen, die aus je einem Fragment der Legumin-a-Ketten und einer intakten P-Kette sowie tryptischen Spaltpeptiden zusammengesetzt sind. Die gelchrornatographisch bestimmte Molmasse betragt (250 1 I ) kDa. Die Aniinosaurezusammensetzung des Legumin-T ist durch eine Erniedrigung des Anteils polarer und eine Erhohung des Anteils uupolarer hydrophober Aminosluren gekennzeichnet. Beide Proteine ergaben iihnliche Werte bei der Messung des zeitlichen Verlaufs der Grenzflachenspannung und der Aufnahme der Kompressionsisothermen. Der fur Legumin-T erhaltene geringere Wert fur das Verhaltnis der bedeckten Grenzflachen A / A , (Legumin = 1, Legumin-T < I ) weist jedoch auf irreversible Desorptionsprozesse der Molekiile des modifizierten Proteins an der GrenzflIche hin. Die Emulgieraktivitat von Legumin-T war hoher als diejenige des nativen Legumins.

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Section: Gelchromatographic Analysissupporting

confidence: 71%

Section: Discussionmentioning

confidence: 80%

Section: Discussionmentioning

confidence: 90%

Section: Gelchromatographic Analysismentioning

confidence: 97%

See 2 more Smart Citations

Legumin‐T from faba bean legumin: Isolation, partial characterization and surface functional properties

Schwenke

Staatz

Dudek

et al. 1995

Nahrung

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“…At present, two models based on the (AB)6 oligomeric structure are postulated for the bean 11 S globulins. According to the model of Plietz et al,26) the acidic subunit is mainly located at the periphery of the protein. A possible TG-reaction site in the basic subunit must be inaccessible to the enzyme in this oligomeric structure because of the shielding effect by the acidic subunit.…”

Section: Sds-pagementioning

confidence: 99%

Gelation of Bean 11S Globulins by Ca²⁺-Independent Transglutaminase

Chanyongvorakul¹,

Matsumura²,

Sakamoto³

et al. 1994

Bioscience, Biotechnology, and Biochemistry

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Acetylation of faba bean legumin: conformational changes and aggregation

Schwenke¹,

Knopfe²,

Seifert

et al. 2000

J. Sci. Food Agric.

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The effect of progressive acetylation upon the conformation of the 11S globulin legumin from faba bean has been studied using chemical analysis, UV, fluorescence and CD spectroscopy, viscometry and analytical ultracentrifugation. The modification did not induce complete dissociation of the oligomeric protein. Only 30% of the protein was found to be a dissociated 3S subunit after excessive acetylation, whereas 70% was a dimeric legumin aggregate with a molecular mass of about 700 kDa. The aggregation of the highly modified legumin in high‐ionic‐strength buffer solution leads to soluble higher legumin oligomers. The acetylation resulted in a moderate molecular expansion of legumin due to a changed tertiary structure, whereas the far‐UV circular dichroism spectra did not provide definitive evidence of a decrease in domain‐stabilizing β‐sheet conformations in their secondary structure. © 2000 Society of Chemical Industry

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Shape, symmetry, hydration and secondary structure of the legumin from Vicia faba in solution

Cited by 63 publications

References 15 publications

Legumin‐T from faba bean legumin: Isolation, partial characterization and surface functional properties

Legumin‐T from faba bean legumin: Isolation, partial characterization and surface functional properties

Gelation of Bean 11S Globulins by Ca²⁺-Independent Transglutaminase

Acetylation of faba bean legumin: conformational changes and aggregation

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Shape, symmetry, hydration and secondary structure of the legumin from Vicia faba in solution

Cited by 63 publications

References 15 publications

Legumin‐T from faba bean legumin: Isolation, partial characterization and surface functional properties

Legumin‐T from faba bean legumin: Isolation, partial characterization and surface functional properties

Gelation of Bean 11S Globulins by Ca2+-Independent Transglutaminase

Acetylation of faba bean legumin: conformational changes and aggregation

Contact Info

Product

Resources

About

Gelation of Bean 11S Globulins by Ca²⁺-Independent Transglutaminase