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
Hauptverfasser: Klotz, Irving M., Fiess, Harold A.
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.
ISSN:0006-3002
1878-2434
DOI:10.1016/0006-3002(60)91195-1