Ultrasonic spectroscopy in bovine serum albumin solutions.
Ultrasonic spectroscopy in bovine serum albumin solutions.
复制标题
牛血清白蛋白溶液中的超声波光谱。
DOI:
10.1121/1.2025804
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发表时间:
1990
期刊:
影响因子:
--
通讯作者:
K. Takagi
中科院分区:
文献类型:
--
作者:
P. Choi;J. Bae;K. Takagi
Ultrasonic absorption and velocity spectra in bovine serum albumin (BSA) aqueous solutions have been measured at 20 degrees C over the broad frequency range 0.1-1600 MHz in the pH range 1.5-13.2. Five different techniques were used: the plano-concave resonator, plano-plano resonator, pulse-echo overlap, Bragg reflection, and high-resolution Bragg reflection methods. The absorption spectrum at neutral pH was well fitted to the relaxation curve assuming a distribution of relaxation frequency with a high-frequency cutoff and long low-frequency tail. The relaxation behavior was interpreted in terms of various degrees of hydration of BSA molecules. At acid pH's, excess absorption over that at pH 7 was explained by double relaxation. The pH dependences of the relaxation frequency and maximum absorption per wavelength showed that the relaxation at about 200 kHz was related to the expansion of molecules and that at 2 MHz resulted from the proton transfer reaction of carboxyl group. At alkaline pH's, the excess absorption was explained by triple relaxation. The relaxation at about 200 kHz was associated with a helix-coil transition, and the two relaxations at 2 and 15 MHz were attributed to the proton transfer reactions of phenolic and amino groups, respectively. The rate constants and volume changes associated with these processes were estimated.