Ionic equilibria in a protein conjugate of a sulfonamide type
The acidity constants of the (CH 3) 2N-group of 5-dimethylamino- i-naphthalene sulfonyl conjugates of glycine and of bovine serum albumin have been compared. In the native protein environment, p K a is shifted by over 2.3 pH units. Denaturation of the protein by 8 M urea reduced the shift in p K a t...
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Veröffentlicht in: | Biochimica et biophysica acta 1960-01, Vol.38, p.57-63 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The acidity constants of the (CH
3)
2N-group of 5-dimethylamino-
i-naphthalene sulfonyl conjugates of glycine and of bovine serum albumin have been compared. In the native protein environment, p
K
a is shifted by over 2.3 pH units. Denaturation of the protein by 8
M urea reduced the shift in p
K
a to 0.9 unit. These and related observations are interpreted in terms of changes in the nature of the hydration lattice of the protein molecule. |
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ISSN: | 0006-3002 1878-2434 |
DOI: | 10.1016/0006-3002(60)91195-1 |