Neutral transition and the environment of the sulfhydryl side chain of bovine plasma albumin

Zurawski, Vincent R.; Foster, Joseph F.

doi:10.1021/bi00714a007

Cited by 94 publications

(51 citation statements)

References 25 publications

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“…This basic form is also favoured with increasing ionic strength. Nikkel and Foster [7] and Zurawski and Foster [2] later showed similar effects of pH on the conformation of bovine serum albumin using NMR spectroscopy to follow the chemically modified albumin molecule. Katz and Klotz [8] and Harmsen et al [3] showed for bovine serum albumin that this N-B transition was effected by calcium ions.…”

mentioning

confidence: 88%

“…Zurawski and Foster [ 2] showed evidence for the existence of two conformational states in bovine serum albumin, the N form mainly occurring at the neutral pH and the B form at higher pH. They call this conformational change, therefore, the neutral-to-base or the N-B transition.…”

mentioning

confidence: 99%

“…Zurawski and Foster [2] considered a pH dependent two state conformational change, which can be represented by N -++_ B +nH ÷…”

mentioning

confidence: 99%

“…1 modified to give log(a/(1 --a)) = log K + npH (2) where K is the equilibrium constant and n the number of protons involved in the change; at pHs0 n is termed the Hill coefficient. The value of n is approximately 0.9 and is almost independent of pH in the absence of Ca 2÷.…”

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confidence: 99%

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Conformational changes in human serum albumin around the neutral pH from circular dichroic measurements

Wilting

Weideman

Roomer

et al. 1979

Biochimica et Biophysica Acta (BBA) - Protein Structure

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SummaryThe molar ellipticity of the warfarin-albumin complex at 310 nm increases with pH from 6 to 9. This pH dependence runs parallel with that of the molar ellipticity of the albumin alone at 292 nm. The change in molar ellipticity with pH occurs in a smaller pH interval after addition of the physiological concentration of calcium ions. These findings give support to the assumption that the binding site for warfarin on the albumin molecule is affected by the neutral-to-base transition in the protein.Several authors have reported a pH dependent conformational change to occur in serum albumin around the physiological pH [1--7]. Zurawski and Foster [ 2] showed evidence for the existence of two conformational states in bovine serum albumin, the N form mainly occurring at the neutral pH and the B form at higher pH. They call this conformational change, therefore, the neutral-to-base or the N-B transition. Leonard et al. [ 1 ] found that the specific rotation of bovine and human serum albumin at 313.2 nm decreases between pH 7 and 9. This was interpreted as a change of the protein structure to another form when the pH was increased. This basic form is also favoured with increasing ionic strength. Nikkel and Foster [7] and Zurawski and Foster [2] later showed similar effects of pH on the conformation of bovine serum albumin using NMR spectroscopy to follow the chemically modified albumin molecule. Katz and Klotz [8] and Harmsen et al. [3] showed for bovine serum albumin that this N-B transition was effected by calcium ions.

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mentioning

confidence: 88%

mentioning

confidence: 99%

“…Zurawski and Foster [2] considered a pH dependent two state conformational change, which can be represented by N -++_ B +nH ÷…”

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Conformational changes in human serum albumin around the neutral pH from circular dichroic measurements

Wilting

Weideman

Roomer

et al. 1979

Biochimica et Biophysica Acta (BBA) - Protein Structure

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“…Concentrations of native BMA solutions were calculated using O. D. 0.1%, lcm 0.667 (27). Concentrations of so-280 nm = lutions of modified BMA were determined by amino acid analysis.…”

Section: Absorption Measurementsmentioning

confidence: 99%

Buoyant titration of bovine mercaptalbumin chemically modified at the carboxyl groups

Svendsen

1976

Carlsberg Res. Commun.

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Bovine mercaptalbumin has been modified at the carboxyl groups by means of I-ethyl-3 (3-dimethylisopropyl) carbodiimide and glycine amide. A stable derivative was obtained after modification of 54 groups. The modified protein differed only slightly from the unmodified one with respect to the optical rotatory dispersion parameters ao, bo and ~. This preparation was studied in the analytical ultracentrifuge in a CsCI gradient in the pH-interval from 2 to 1 I. The buoyant densities were determined and compared with those of the unmodified protein in the same pH-interval. The contribution from the carboxyl groups to the buoyant density is discussed and compared with results obtained with other proteins and synthetic polypeptides.

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Hydration Dynamics and Coupled Water–Protein Fluctuations Probed by Intrinsic Tryptophan

Zhong

2009

Advances in Chemical Physics

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Neutral transition and the environment of the sulfhydryl side chain of bovine plasma albumin

Cited by 94 publications

References 25 publications

Conformational changes in human serum albumin around the neutral pH from circular dichroic measurements

Conformational changes in human serum albumin around the neutral pH from circular dichroic measurements

Buoyant titration of bovine mercaptalbumin chemically modified at the carboxyl groups

Hydration Dynamics and Coupled Water–Protein Fluctuations Probed by Intrinsic Tryptophan

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