Many gluten components have been reported, but their physicochemical properties are rarely reported due to the small amount of preparation. In this research, ω-gliadin, αβγ-gliadin, alkali-soluble and urea-soluble glutenin (ASG and USG) fractions were isolated by conventional methods and characterized by molecular weights, disulfide bond contents, amino acid compositions, Ultraviolet (UV) absorption, FTIR and 13C Solid-state NMR Spectroscopy. The results showed that purified ω-gliadin, αβγ-gliadin, ASG and USG could be obtained by conventional methods on a large scale (approximately 9.67 %, 12.43 %, 6.00 % and 18.26 %, respectively). The UV absorption of gluten components in the helical and randomly coiled state could not be detected. The molecular weights of purified ω-gliadin, αβγ-gliadin, ASG and USG were all ∼38,500 g/mol and their disulfide bond contents were 0.076, 0.374, 0.086 and 0.576 μmol/g, respectively. USG is characterized by free Glu and redundant Met, Phe and Ile. The distinctively diffraction angles of the gluten component monomers were 2θ at 22 °, 24 °, 29 ° and 35 °. This study will be of great reference value for the industrial application of these newly isolated proteins in gluten production.