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S Era

Publications and source records attributed to S Era.

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Circular dichroic and fluoropolarimetric studies on tryptophyl residues in acid-induced isomerization of bovine plasma albumin.

The acid-induced isomerization (the N-F transition) and expansion of bovine plasma albumin were studied by measuring circular dichroic spectra and fluorescence polarization of tryptophyl residues. Decreases in the magnitude of ellipticities at 208, 222, 262 and 268 nm were observed in the N-F transition and acid-expansion. However, increases in the magnitude of ellipticities at 295-300 nm observed in the initial part of the N-F transition exactly correlated with the increase of rotational relaxation time of tryptophyl side chains obtained by fluorescence polarization measurement.

Animals↗

Conformational changes of bovine plasma albumin prior to the salting-out of protein in concentrated salt solution.

By working at very low protein concentration (ca. 0.003%), it is possible to measure tryptophyl fluorescence intensity at 350 nm (F350) of bovine plasma albumin (BPA) as a function of pH under precipitating conditions (acidic concentrated salt solutions). Under such conditions, distinct changes in F350 were seen before the starting of precipitation of BPA and no further changes in F350 over the precipitating pH range. Comparison of pH-profiles monitored by F350 with those by solubility in the presence of various salts at various concentrations indicated that the change of solubility is observed after definite changes in conformation of the protein.

Animals↗