Resonance-enhanced Raman spectra of visual pigments in intact bovine retinas at low temperatures.
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Biomedical subjects
Publications and source records attributed to L Rimai.
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Using measurements of quasi-elastic light scattering spectra, we have investigated diffusional fluctuations of RNase. The diffusion coefficient for individual protein molecules, together with the corresponding calculated effective molecular radius R(eff), were determined. Between room temperature and the point of irreversible denaturation at 63.5 degrees C, R(eff) increased from 20-250 A. This is comparable to the plateau in R(eff) of 300 A reached after about 200 min following chemical denaturation in 10 M urea. The measurements indicated the presence of a large size component even in the freshly prepared and chromatographically purified solutions. From the diffusion constants deduced for this large component we obtained effective sizes from 1000-5000 A. Concentration and temperature dependent measurements exclude the possibility that these large particles are impurities and indicate that they are the result of aggregations of RNase molecules.
Using a He-Ne CW laser source together with a digital photon counting system, we have obtained well resolved Raman spectra for adenosine mono-, di-, and triphosphate (AMP, ADP, ATP) in aqueous solution. Spectra of these compounds were studied as a function of pH from pH = 0.5 to 13.5 and between 550 and 1700 cm(-1). It was found possible to distinguish spectroscopically between the three phosphates over the pH range studied. A qualitative analysis of vibrational modes responsible for various spectral lines is given. Lines at about 960 and 1100 cm(-1) were found to be good indications of the degree of ionization of the terminal phosphate group.