Fluorescence studies of two γ-gliadin fractions from bread wheat

N. A. Yeboah; R. B. Freedman; Y. Popineau; P. R. Shewry; A. S. Tatham

doi:10.1006/jcrs.1994.1019

Fluorescence studies of two γ-gliadin fractions from bread wheat

N. A. Yeboah^*, R. B. Freedman, Y. Popineau, P. R. Shewry, A. S. Tatham

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

12 Citations (Scopus)

Abstract

Two γ-gliadin fractions, designated γ_III and γ_V, were purified from cv. Chinese Spring and shown by N-terminal amino acid sequencing to be typical γ-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.

Original language	English
Pages (from-to)	141-148
Number of pages	8
Journal	Journal of Cereal Science
Volume	19
Issue number	2
DOIs	https://doi.org/10.1006/jcrs.1994.1019
Publication status	Published - Mar 1994
Externally published	Yes

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AU - Shewry, P. R.

AU - Tatham, A. S.

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AB - Two γ-gliadin fractions, designated γIII and γV, were purified from cv. Chinese Spring and shown by N-terminal amino acid sequencing to be typical γ-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.

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Fluorescence studies of two γ-gliadin fractions from bread wheat

Abstract

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