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Preparative isoelectric focusing of reduced wheat gluten proteins.
Electrophoresis. 1990 Jun; 11(6):462-7.E

Abstract

Proteins extracted from gluten of the bread wheat cultivar Fiorello 2 in the presence of 2-mercaptoethanol or dithiothreitol were separated by isoelectric focusing in a free solution in a pH 3-10 gradient containing 50% v/v 1-propanol or urea. The collected fractions were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in 10% gels (high and medium molecular weight glutenin subunits) and 16% gels (low molecular weight gliadins). The isoelectric focusing pattern of gluten polypeptides in 50% v/v 1-propanol was comparable to that obtained on two-dimensional gel electrophoresis, based on isoelectric focusing and polyacrylamide gel electrophoresis or nonequilibrium pH gradient electrophoresis and polyacrylamide gel electrophoresis. A similar isoelectric focusing pattern was also observed when 3M urea was used as solvent. New gluten polypeptides, similar in mobility to the high molecular weight subunits of glutenin were detected at acidic pH.

Authors+Show Affiliations

Curioni A
University of Padua, Dipartimento di Biotecnologie Agrarie, Padova, Italy.
Dal Belin Peruffo A
No affiliation info available
Pogna NE
No affiliation info available

MeSH

1-PropanolAlkylationElectrophoresis, Polyacrylamide GelGlutensHydrogen-Ion ConcentrationIsoelectric FocusingOxidation-ReductionTriticumUrea

Pub Type(s)

Journal Article

Language

eng

PubMed ID

2394208

Citation

Curioni, A, et al. "Preparative Isoelectric Focusing of Reduced Wheat Gluten Proteins." Electrophoresis, vol. 11, no. 6, 1990, pp. 462-7.
Curioni A, Dal Belin Peruffo A, Pogna NE. Preparative isoelectric focusing of reduced wheat gluten proteins. Electrophoresis. 1990;11(6):462-7.
Curioni, A., Dal Belin Peruffo, A., & Pogna, N. E. (1990). Preparative isoelectric focusing of reduced wheat gluten proteins. Electrophoresis, 11(6), 462-7.
Curioni A, Dal Belin Peruffo A, Pogna NE. Preparative Isoelectric Focusing of Reduced Wheat Gluten Proteins. Electrophoresis. 1990;11(6):462-7. PubMed PMID: 2394208.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Preparative isoelectric focusing of reduced wheat gluten proteins. AU - Curioni,A, AU - Dal Belin Peruffo,A, AU - Pogna,N E, PY - 1990/6/1/pubmed PY - 1990/6/1/medline PY - 1990/6/1/entrez SP - 462 EP - 7 JF - Electrophoresis JO - Electrophoresis VL - 11 IS - 6 N2 - Proteins extracted from gluten of the bread wheat cultivar Fiorello 2 in the presence of 2-mercaptoethanol or dithiothreitol were separated by isoelectric focusing in a free solution in a pH 3-10 gradient containing 50% v/v 1-propanol or urea. The collected fractions were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in 10% gels (high and medium molecular weight glutenin subunits) and 16% gels (low molecular weight gliadins). The isoelectric focusing pattern of gluten polypeptides in 50% v/v 1-propanol was comparable to that obtained on two-dimensional gel electrophoresis, based on isoelectric focusing and polyacrylamide gel electrophoresis or nonequilibrium pH gradient electrophoresis and polyacrylamide gel electrophoresis. A similar isoelectric focusing pattern was also observed when 3M urea was used as solvent. New gluten polypeptides, similar in mobility to the high molecular weight subunits of glutenin were detected at acidic pH. SN - 0173-0835 UR - https://www.unboundmedicine.com/medline/citation/2394208/Preparative_isoelectric_focusing_of_reduced_wheat_gluten_proteins_ DB - PRIME DP - Unbound Medicine ER -