| Autor: |
McCarty BW; Chemistry Department, Texas A&M University, College Station 77843., Adams ET Jr |
| Jazyk: |
angličtina |
| Zdroj: |
Biophysical chemistry [Biophys Chem] 1987 Nov; Vol. 28 (2), pp. 149-59. |
| DOI: |
10.1016/0301-4622(87)80084-4 |
| Abstrakt: |
Ovalbumin and lysozyme have been reported to undergo a mixed association in solutions of low ionic strength. Osmotic pressure experiments were performed on ovalbumin and on lysozyme solutions in 0.06 M cacodylate buffer (I = 0.02, pH = 5.8) at 30 and at 37 degrees C. The individual proteins did not undergo any self-associations at either temperature; these measurements indicated that each of the solutions was nonideal. Osmotic pressure experiments on three blends of lysozyme and ovalbumin at 30 and 37 degrees C could be interpreted in two ways. One interpretation was that a nonideal, nonassociating mixture of A and B was present; for the three solutions the mixed nonideal term BAB was negative. A negative nonideal term is usually interpreted as indicating an association. The other interpretation of the data was as a quasi-ideal mixed association of the type A + B in equilibrium AB. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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