Effects of polysaccharides upon the functional properties of 11 S globulin of broad beans

Burova, Tatiana V.; Grinberg, Natalia V.; Grinberg, V. Ya.; Leontiev, A.L.; Tolstoguzov, V. B.

doi:10.1016/0144-8617(92)90131-9

Cited by 29 publications

(11 citation statements)

References 16 publications

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“…Thus the conformational stability of lysozyme decreases in result of its binding to the NIPA–SSS copolymer matrix. The similar effect was mentioned for some globular proteins bound to polyelectrolytes 17, 18, 30. It was explained by the preferential binding of the unfolded protein form to the polymer matrix.…”

Section: Resultssupporting

confidence: 68%

Binding Energetics of Lysozyme to Copolymers of N‐Isopropylacrylamide with Sodium Sulfonated Styrene

Burova

Grinberg

et al. 2009

Macromolecular Bioscience

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Interpolyelectrolyte complexes of lysozyme with thermosensitive N-isopropylacrylamide-sodium sulfonated styrene copolymers of different charge density were investigated by high-sensitivity differential scanning calorimetry (HS-DSC) at pH 4.6-7.2 and low ionic strength. A general property of the complexes for all copolymers investigated was a decrease in the conformational stability of the bound protein. This suggested the preferential binding of the unfolded protein to the polymer matrix. The isotherms of lysozyme binding to the copolymers were derived from the HS-DSC data. They indicate that the binding is irreversible and charge stoichiometric.

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Section: Resultssupporting

confidence: 68%

Binding Energetics of Lysozyme to Copolymers of N‐Isopropylacrylamide with Sodium Sulfonated Styrene

Burova

Grinberg

et al. 2009

Macromolecular Bioscience

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“…Similar effects were observed for other protein-poly electrolyte systems [22][23][24][25][26]. The probable cause of enzyme destabilization is that the unfolded protein is preferably bound by the polymer matrix [23,45].…”

Section: Conformational Stability Of Soybean Peroxidase and The Nipa-supporting

confidence: 55%

“…These centers may be neg atively or positively charged groups, specifically, car boxyl, sulfonate, or trimethylammonium. Despite a considerable bulk of studies dealing with the inter polyelectrolyte complexes of proteins [22][23][24][25][26], the systematic data on conformational changes in ther moresponsive polymers and globular proteins result ing from complexation are very scanty. There are almost only single facts derived by indirect methods [27][28][29][30].…”

Section: Introductionmentioning

confidence: 99%

Interpolyelectrolyte complexes of soybean peroxidase with thermoresponsive copolymers

et al. 2012

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Interpolyelectrolyte complexes of soybean peroxidase with thermoresponsive N isopropylacryla mide-sodium styrenesulfonate copolymers of various compositions are studied by the methods of high sen sitivity differential scanning calorimetry, velocity sedimentation, and nephelometry. It is shown that the enzyme preserves its tertiary structure in complexes, although the conformational stability of bound protein is lower than that of free protein. Complexes of any compositions, including stoichiometric complexes, are soluble at room temperature but precipitate during heating in the region of the conformational transition of the copolymer accompanied by formation of the complex gel. Isotherms of enzyme binding by complex gels are constructed, and their analysis makes it possible to reveal two types of binding in the system: a relatively strong stoichiometric binding of the enzyme with the copolymers and a weaker binding of the protein in the coacervate phase of the complex gel. A high yield of the protein in the complex gel, reversibility of binding, and preservation of the tertiary structure of the enzyme in complexes with the copolymers make proteinthermoresponsive polyelectrolyte systems promising for bioseparation.

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“…The experimental conditions utilised corresponded to either the incompatibility of STI and polysaccharides or to their complexation. [19][20][21][22][23][24][25][26][27][28][29] Experimental Part Materials STI from soybean (type T-9003) was purchased from Sigma and used without further purification. According to velocity sedimentation data and gel electrophoresis, the homogeneity of the preparation was > 97%.…”

Section: Introductionmentioning

confidence: 99%

Effect of polysaccharides on the stability and renaturation of soybean trypsin (Kunitz) inhibitor

et al. 2002

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Effects of polysaccharides upon the functional properties of 11 S globulin of broad beans

Cited by 29 publications

References 16 publications

Binding Energetics of Lysozyme to Copolymers of N‐Isopropylacrylamide with Sodium Sulfonated Styrene

Binding Energetics of Lysozyme to Copolymers of N‐Isopropylacrylamide with Sodium Sulfonated Styrene

Interpolyelectrolyte complexes of soybean peroxidase with thermoresponsive copolymers

Effect of polysaccharides on the stability and renaturation of soybean trypsin (Kunitz) inhibitor

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