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BERYLLIUM BINDING BY BOVINE SERUM ALBUMIN AT ACID pH

Journal Article · · Journal of the American Chemical Society (U.S.)
DOI:https://doi.org/10.1021/ja00897a026· OSTI ID:4696529
The binding of beryllium by bovine serum albumin was investigated, at three temperatures, in the pH region 5 and below', where beryllium salts are soluble and dialyzable. Reversible association was studied by the method of equilibrium dialysis in solutions containing nitrate ion at an ionic strength of 0.15. The amount of binding increased with increasing pH and temperature. The constancy of the intrinsic association constant (K = 36.2) and the variation of n, the number of binding sites, suggest that environmental conditions modfy the structure of the protein so that a varying number of a single class of binding sites become available for reaction. Considerations of the effect of pH and temperatare on beryllium ion hydrolysis and albumin structure support this interpretation. Esterified serum albumin exhibited no beryllium binding, which is evidence for the carboxyls as the reacting groups. The results of potentiometric titrations agreed with those obtained from equilibrium dialysis. Albumin denatured by dodecyl sulfate showed greatly increased beryllium binding, which was attributed to the electrostatic effect of the bound anion. The cooperative behavior of the beryllium binding was ascribed to the structural effects induced by dodecyl sulfate bound to albumin. Although the beryllium species in equilibrium with the protein is unknown, the data suggest that Be/sup 2+/ is one reacting species. (auth)
Research Organization:
New York Univ., New York
Sponsoring Organization:
USDOE
NSA Number:
NSA-17-030261
OSTI ID:
4696529
Journal Information:
Journal of the American Chemical Society (U.S.), Journal Name: Journal of the American Chemical Society (U.S.) Vol. Vol: 85; ISSN JACSA
Country of Publication:
Country unknown/Code not available
Language:
English

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