Fluorescenc Studies of 2 Gamma-Gliadin Fractions form Bread Wheat

Two gamma-gliadin fractions, designated gamma(III) and gamma(V), were purified from cv. Chinese Spring and shown by N-terminal amino acid sequencing to be typical gamma-gliadin types. Fluorescence spectroscopy of the gliadin fractions under non-denaturing conditions indicated that the tryptophan residues were exposed to the solvent. Under denaturing conditions only small changes were observed in fluorescence intensity and maximum emission wavelength, confirming that the tryptophan residues were exposed to the solvent prior to denaturation. Time-resolved fluorescence measurements gave rotational correlation times of 3-6 ns, indicating a high degree of mobility.