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• W2013992091 abstract "Electron micrographs have been obtained of bovine serum albumin in solutions of low ionic strength at pH values in the range 1·9 to 6·9. The predominant form of the molecule at neutral pH is found to be a globular particle approximately 60 Å in diameter and 45 Å high. Below pH 4, the molecule extends to a threadlike form which measures approximately 250 Å long and 21 A in diameter at pH 1·9. While the details of the substructure of the acid form of serum albumin are below the resolution limit of the shadowing technique, micrographs indicate that extension must have occurred at several regions within the molecule. Compact doublet monomers are believed to be intermediates in the acid denaturation; similar structures also appear to be formed from native molecules as artifacts of specimen preparation. The proportions of native and denatured particle types found in micrographs of serum albumin are found to change with pH in the same manner as do hydrodynamic properties of the molecule. The configurational change is found to be reversible, and to be complete within 24 seconds after acidification of the albumin solution." @default.
• W2013992091 created "2016-06-24" @default.
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• W2013992091 date "1965-12-01" @default.
• W2013992091 modified "2023-10-18" @default.
• W2013992091 title "An electron microscope study of the conformational change in bovine serum albumin at low pH" @default.
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• W2013992091 doi "https://doi.org/10.1016/s0022-2836(65)80194-2" @default.
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