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Denaturation of bovine serum albumin


, : Denaturation of bovine serum albumin. Fed Proc 11(1): 248



Accession: 024449733

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Related references

Takeda, K.; Hamada, S.; Wada, A., 1993: Secondary structural changes of large and small fragments of bovine serum albumin in thermal denaturation and in sodium dodecyl sulfate denaturation. The helicities in various fragments of bovine serum albumin (BSA) were examined in the thermal denaturation and in sodium docecyl sulfate (SDS) denaturation. The thermal denaturation was examined in a temperature range between 2 and 65 degree C. T...

Kapoor, R.C., 1960: Urea denaturation of bovine serum albumin. Denaturation studies of bovine serum albumin have been made using urea as the denaturating agent. The concentration used was 6 [image] urea. The change in the reactivity of sulphydryl group has been observed amperometrically using a rotating plati...

Aoki, K.; Murata, M.; Hiramatsu, K., 1974: Urea denaturation of bovine serum albumin at pH 9. Analytical Biochemistry 59(1): 146-157

Precupas, A.; Sandu, R.; Popa, V.T., 2016: Quercetin Influence on Thermal Denaturation of Bovine Serum Albumin. The effect of quercetin (QUER) binding on bovine serum albumin (BSA) thermal denaturation was systematically investigated by means of differential scanning calorimetry (DSC). Additional information concerning thermodynamic and structural binding p...

Aoki, K.; Sato, K.; Nagaoka, S.; Kamada, M.; Hiramatsu, K., 1973: Heat denaturation of bovine serum albumin in alkaline pH region. The heat denaturation of bovine serum albumin was studied at 65°C in 0.1 M Tris-EDTA-boric acid buffer at pH 9.0. The gel electrophoresis indicated that the heat-treated bovine serum albumin solution contained several components, 1, 1, 2, 3 and o...

Alexander, P.; Hamilton, L.D., 1960: Changes in the reactivity of disulfide bonds in bovine serum albumin on denaturation. Earlier observations showing that in native bovine serum albumin (BSA) none of the disulfide bonds can be reduced at pH 5.4 were confirmed. They were resistant to oxidation by dilute peracetic acid, proving that failure to react must be ascribed t...

Bummer, P.M.; Traboulsi, A.; Foshee, M., 1992: Air-water interface-induced denaturation of bovine serum albumin. Pharmaceutical Research (New York) 9(10 SUPPL ): S185

Harmsen, B.J.; Braam, W.G., 1969: On the conformation of bovine serum albumin after alkaline or thermal denaturation. International Journal of Protein Research 1(4): 225-233

Borzova, V.A.; Markossian, K.A.; Chebotareva, N.A.; Kleymenov, S.Yu.; Poliansky, N.B.; Muranov, K.O.; Stein-Margolina, V.A.; Shubin, V.V.; Markov, D.I.; Kurganov, B.I., 2016: Kinetics of Thermal Denaturation and Aggregation of Bovine Serum Albumin. Thermal aggregation of bovine serum albumin (BSA) has been studied using dynamic light scattering, asymmetric flow field-flow fractionation and analytical ultracentrifugation. The studies were carried out at fixed temperatures (60°C, 65°C, 70°C...

Alexander, P.; Hamilton, L.D.G., 1960: Changes in the reactivity of disulphide bonds in bovine serum albumin on denaturation. Earlier observations showing that in native bovine serum albumin (BSA) none of the disulfide bonds can be reduced at pH 5.4 were confirmed. They were resistant to oxidation by dilute peracetic acid, proving that failure to react must be ascribed t...