On the Interaction of Some Proteins with Sulfonated Dextran in an Aqueous Medium

Gurov, A. N.; Wajnerman, E. S.; Tolstoguzov, V. B.

doi:10.1002/star.19740260507

Cited by 19 publications

(3 citation statements)

References 2 publications

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“…As shown in Figure C, D a for the mixtures increases from 170 to 260 nm with PIMA concentration. It has been pointed out that the charge fluctuations determine an ability of proteins to be bound to polyanions even in the vicinity of pI, resulting in solubilization of protein under such conditions. , In the mixture solution with PIMA concentration of 4.5 × 10 -6 g/mL, the complex particles become smaller than apo cyt c , suggesting that the very low concentration of PIMA may inhibit the aggregation of apo cyt c . The net charges of apo cyt c are about zero and PIMA carries about 68 negative charges averagely, so the negative charges of PIMA are on the surface of the complex particles to stabilize them.…”

Section: Resultsmentioning

confidence: 99%

Interactions of Apo Cytochromecwith Alternating Copolymers of Maleic Acid and Alkene

Liang¹,

Yao²,

Jiang³

et al. 2005

Langmuir

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Apo cytochrome c (apo cyt c) tends to aggregate at alkali pH. Poly(isobutylene-alt-maleic acid) (PIMA) is soluble molecularly, whereas poly(1-tetradecene-alt-maleic acid) (PTMA) forms particles that tend to dissociate by increasing pH and decreasing concentration. Dynamic light scattering and surface plasmon resonance are used to investigate the interactions of PIMA and PTMA with apo cyt c at different pH values to understand the mechanism of the interactions. When the positive or negative charges are in excess, the copolymer-protein complex particles can be stabilized by the charges on the surface. When the ratio of the positive to negative charges is close to the stoichiometric value, precipitation occurs. At pH 11.8, both PTMA and apo cyt c carry negative charges, but the hydrophobic interaction makes them form complexes. A competition exists between the interaction of the copolymer with apo cyt c and the self-aggregation of PTMA or apo cyt c alone. The interaction of PIMA or PTMA with apo cyt c at neutral and alkali pH destroys the aggregation of PTMA or apo cyt c and forms new complex particles.

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Section: Resultsmentioning

confidence: 99%

Interactions of Apo Cytochromecwith Alternating Copolymers of Maleic Acid and Alkene

Liang¹,

Yao²,

Jiang³

et al. 2005

Langmuir

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“…[32] Acid polysaccharides may also form soluble polyelectrolyte complexes with proteins at pH values below their isoelectric point. [19,20,23,24,29] Conformational stability of STI was investigated under conditions of complexation using the systems STI/dextran sulfate and STI/pectin. The former can be considered as a model system while the latter represents a subject of potential practical significance.…”

Section: High-sensitivity Differential Scanning Calorimetry (Hs-dsc)mentioning

confidence: 99%

“…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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Wechselwirkung zwischen Proteinen und sauren Polysacchariden

Wainerman¹,

Gurow²,

Tolstogusow³

et al. 1975

Nahrung

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The intereaction between proteins and acid polysaccharides is electrostatic in nature and leads to the formation of soluble charged and insoluble neutral complexes. The complex formation in the system casein-dextran sulphate is followed by means of turbidimetric titration. It depends on the pH value and the electrolyte concentration. On free electrophoresis, complexes formed below the isoelectric point of the protein exhibit anodic mobility, whereas pure casein migrates to the cathode. The protein in the complex is not able to bind amido black. Consequently, it cannot be detected electrophoretically by dyebinding. The results from viscosity and diffusion measurements are indicative of an increased hydrodynamic volume of the complexes.

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On the Interaction of Some Proteins with Sulfonated Dextran in an Aqueous Medium

Cited by 19 publications

References 2 publications

Interactions of Apo Cytochromecwith Alternating Copolymers of Maleic Acid and Alkene

Interactions of Apo Cytochromecwith Alternating Copolymers of Maleic Acid and Alkene

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

Wechselwirkung zwischen Proteinen und sauren Polysacchariden

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