Reformation of the Helical Structure of Bovine Serum Albumin by the Addition of Small Amounts of Sodium Dodecyl Sulfate after the Disruption of the Structure by Urea

Moriyama, Yoshiko; Sato, Yasuhiro; Takeda, Kunio

doi:10.1006/jcis.1993.1132

Cited by 42 publications

(53 citation statements)

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“…At the mixing ratios of [AOT]/[HSA] of 5 to 15, similar effects have been observed on the HSA structure at 65˚C 28) . In addition, similar protection and recovery have been observed at the mixing ratios below 10mol/mol in urea denaturation 29,30) as well. It should be noted that actual binding numbers of surfactant ion to the protein are necessarily smaller than the mixing ratios of the surfactant concentration where these prominent effects are observed.…”

Section: Effect Of Gemini Surfactant On Bsa Structure In Thermal Denasupporting

confidence: 51%

Protective Effect of Gemini Surfactant on Secondary Structural Change of Bovine Serum Albumin in Thermal Denaturation up to 130.DEG.C

2009

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The effect of gemini surfactant, sodium dilauramidoglutamide lysine (DLGL), on the secondary structure of bovine serum albumin (BSA) was examined at 25˚C and at high temperatures up to 130˚C. The helicity (66%) of the protein decreased to 53% in the DLGL solution at 25˚C and it also decreased to 16% with rise of temperature. Although approximately half of the original helical structures were destroyed upon heating up to 75˚C, most of the structures were maximally protected in the coexistence of 0.30mM DLGL at 75˚C (the protein concentration was 0.010mM). At temperatures below 75˚C, the protected helicity became maximal at such low DLGL concentrations. In the thermal denaturations above 80˚C, the protective effect did not appear at low DLGL concentrations, but monotonously enlarged with the surfactant concentration. On the other hand, upon cooling to 25˚C after the thermal denaturations below 75˚C, the helicity was maximally recovered to about 60% in the presence of DLGL below 0.30mM. Upon cooling to 25˚C from high temperatures above 85˚C, the recovered helicity gradually increased with the surfactant concentration. The present novel effect, especially observed at low DLGL concentrations, might be fulfilled by the monomer ions of the gemini surfactant, since actual binding numbers of DLGL onto BSA are necessarily smaller than the mixing ratios around 30mol/mol.

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Section: Effect Of Gemini Surfactant On Bsa Structure In Thermal Denasupporting

confidence: 51%

Protective Effect of Gemini Surfactant on Secondary Structural Change of Bovine Serum Albumin in Thermal Denaturation up to 130.DEG.C

2009

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“…27 However, attention should be paid to the small differences in their structures in discussing the correlation between structure and binding properties. 10,28,29 Binding of CnX to HSA Figure 2 shows the effects of CnX on the fluorescence intensity of ANS-HSA solution, in which the fluorescence intensity was plotted as a function of the total concentration of CnX, [CnX]total.…”

Section: Resultsmentioning

confidence: 99%

Binding Properties of Hydrophobic Molecules to Human Serum Albumin Studied by Fluorescence Titration

et al. 2009

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Two fluorescence modes were combined to analyze the binding properties of terminally substituted alkanes (CnX, X = COOH, OH, CHO, NH2) to human serum albumin (HSA). A competitive binding assay using an 8-anilino-1-naphthalenesulfonate (ANS) fluorescence probe provides information on all the hydrophobic binding sites in HSA. A binding assay using the intrinsic fluorescence of the tryptophan residue in HSA (Trp-HSA) provides information on the specific binding site close to the tryptophan residue. There are three fluorescence-active ANS binding sites in HSA, which can be classified into two types by their affinity for ANS. CnCOOH bound to all three ANS binding sites including the Trp-HSA site, however, it did not quench the fluorescence of Trp-HSA. CnCHO bound only to the Trp-HSA site with quenching of the fluorescence of Trp-HSA. By comparing the binding affinities of HSA for CnOH and CnCHO, it was concluded that the CnOH binding site is different from the CnCHO binding site. CnNH2 did not bind to any of the three ANS binding sites in HSA.

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“…265 Moriyama et al, 1993;Takeda et al, 1981Takeda et al, , 1987Takeda et al, , 1988aTakeda et al, , 1989 and HSA (Honor6 and Frandsen, 1986;Honor6 and Pedersen, 1989;Strop et al, 1984;'t Hart et al, 1986;Wetzel et al, 1980) in various conditions. Through these studies, it has become clear that BSA and HSA are homologous proteins composed of single polypeptide chains with 583 (Carter and Ho, 1994;Hirayama et al, 1990) and 585 amino acids (Brown, 1977;Carter and Ho, 1994;Hirayama et al, 1990), respectively.…”

Section: Introductionmentioning

confidence: 99%

Fluorescence behavior of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: A comparative study of the two and one tryptophan(s) of bovine and human albumins

et al. 1996

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The fluorescence behavior of two tryptophans (Trp-134, Trp-213) in bovine serum albumin (BSA) and a single tryptophan (Trp-214) in human serum albumin (HSA) was examined. The maximum emission wavelength (lambda max) was 340.0 nm for both proteins. In a solution of sodium dodecyl sulfate (SDS), the lambda max of BSA abruptly shifted to 332 nm at 1 mM SDS and then reversed to 334 nm at 3 mM SDS. The lambda max of HSA gradually shifted to 330 nm below 3 mM SDS, although it returned to 338 nm at 10 mM SDS. In contrast to this, in a solution of dodecltrimethylammonium bromide, the lambda max positions of BSA and HSA gradually shifted to 334.0 and 331.5 nm, respectively. Differences in the fluorescence behavior of the proteins are attributed to the fact that Trp-134 exists only in BSA, with the assumption that Trp-213 of BSA behaves the same as Trp-214 of HSA. The Trp-134 behavior appears to relate to the disruption of the helical structure in the SDS solution.

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Reformation of the Helical Structure of Bovine Serum Albumin by the Addition of Small Amounts of Sodium Dodecyl Sulfate after the Disruption of the Structure by Urea

Cited by 42 publications

References 0 publications

Protective Effect of Gemini Surfactant on Secondary Structural Change of Bovine Serum Albumin in Thermal Denaturation up to 130.DEG.C

Protective Effect of Gemini Surfactant on Secondary Structural Change of Bovine Serum Albumin in Thermal Denaturation up to 130.DEG.C

Binding Properties of Hydrophobic Molecules to Human Serum Albumin Studied by Fluorescence Titration

Fluorescence behavior of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: A comparative study of the two and one tryptophan(s) of bovine and human albumins

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