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Biomedical subjects

H Terada

Publications and source records attributed to H Terada.

At least 361 records · Page 20Linked to original sources
PubMed1980

Heat denaturation of serum albumin monitored by 1-anilino-naphthalene-8-sulfonate.

The process of heat denaturation of serum albumin, and the properties of several denatured components of albumin were studied using 1-anilino-naphthalene-8-sulfonate as a probe dye. Like native albumin, these protein species all induce fluorescence of the dye with maximum emission at 470 nm when excited at 380 nm. However, the affinity of albumin for the dye decreased on denaturation. This fluorescent dye bound competitively to both native and denatured albumin with another probe dye, 2-(4'-hydroxyphenylazo)benzoic acid, has a specific absorption band at about 480 nm on binding with native albumin. Fatty acids, such as lauric acid, inhibited the interaction of 1-anilinonaphthalene-8-sulfonate with native albumin, but had little effect on its binding with denatured albumin.

Anilino Naphthalenesulfonates↗
PubMed1979

Estimation of state and amount of phenylalanine residues in proteins by second derivative spectrophotometry.

The second derivative absorption spectra of serum albumin, insulin, ribonuclease and lysozyme were measured under various conditions to determine the state and amount of their phenylalanine residues. The second derivative spectra of these proteins were very similar to that of phenylalanine in the region between 245 and 270 nm where tryptophan and tyrosine residues caused no appreciable interference. Denaturation of proteins with urea or guanidine hydrochloride caused decrease in the intensity of the second derivative spectra, but scarcely affected the positions of peaks and troughs. The amounts of phenylalanine residues in proteins calculated from a second derivative spectra of denatured proteins coincided well with those reported in the literature. The states of the phenylalanine residues in the proteins could be deduced from the change in optical intensity on denaturation.

Chemical Phenomena↗