Thermodynamic stability of bovine alpha-crystallin in its interactions with other bovine crystallins.
Light scattering measurements were performed on dilute solutions of alpha-crystallin mixed with different combinations of beta H, beta L and gamma-fractions of bovine lens crystallins. Light scattering intensities were obtained as a function of scattering angle, concentration and temperature. The temperature dependence of the second virial coefficients was used to obtain partial molar enthalpy and end entropy of solutions. The difference between the thermodynamic parameters of the crystallin mixtures and those of the weighted averages of the individual components yielded the excess enthalpy and entropy functions of the solutions. Both the excess enthalpy and entropy functions indicated that thermodynamic stability of alpha-crystallin is progressively enhanced by its interactions with gamma [symbol: see text] (beta H + gamma) [symbol: see text] (beta H + beta L + gamma) crystallins. The last two combinations showed negative values both for excess enthalpy as well for excess entropy of solutions. Other combinations demonstrated increasing positive values. This implies that the combination of all four crystallins in the vertebrate lens enables the best solvation property as well as the best packing as opposed to any other single or combinatorial arrangements of crystallins. Similar conclusions have been obtained in the past from water and other vapor sorption studies.
Bettelheim
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FA
Chemistry Department, Adelphi University, Garden City, NY 11530, USA. Bettelhe@Adlibv.Adelphi.edu
Chen
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A
D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000737:chemistry*; D004355:Drug Stability; D019277:Entropy; D008027:Light; D046911:Macromolecular Substances; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012542:Scattering, Radiation; D012996:Solutions; D013816:Thermodynamics
D003459:Crystallins; D046911:Macromolecular Substances; D012996:Solutions