Multiple Zeins from Maize Endosperms Characterized by Reversed-Phase High Performance Liquid Chromatography
Open Access
- 1 March 1991
- journal article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 95 (3) , 777-786
- https://doi.org/10.1104/pp.95.3.777
Abstract
The major storage proteins of maize (Zea mays L.) endosperm are located in protein bodies, and may be separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) into two major classes and four minor classes of polypeptides. The two major classes (commonly known as zeins) have been separated previously into a large number of components by isoelectric focusing (IEF). Reversed-phase high performance liquid chromatography (HPLC) further separated the major classes into additional components, and gave distinctive peaks for each minor zein class. Some IEF bands produced two or more HPLC fractions, while some HPLC fractions produced two or more IEF bands. Apparently identical IEF bands from different inbreds may appear in different fractions after HPLC. Thus the total number of zeins revealed by separations based on apparent size (SDS-PAGE), net charge (IEF), and hydrophobicity (HPLC) is very large. Different laboratories have developed diverse nomenclatures which cause much confusion. A key is presented to provide a flexible and expandable nomenclature for this complex group of proteins.Keywords
This publication has 15 references indexed in Scilit:
- New Methods for Extraction and Quantitation of Zeins Reveal a High Content of γ-Zein in Modified opaque-2 MaizePlant Physiology, 1990
- Structural elements regulating zein gene expressionBioEssays, 1989
- Isolation and sequence of a gene encoding a methionine-rich 10-kDa zein protein from maizeGene, 1988
- Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G‐250 and R‐250Electrophoresis, 1988
- Multiple variability in the sequence of a family of maize endosperm proteinsGene, 1987
- Serial Analysis of Zein by Isoelectric Focusing and Sodium Dodecyl Sulfate Gel ElectrophoresisPlant Physiology, 1986
- Primary Structure of a Proline-Rich Zein and Its cDNAPlant Physiology, 1986
- Separation of Alcohol-Soluble Proteins (Zeins) from Maize into Three Fractions by Differential SolubilityPlant Physiology, 1986
- An enzyme-linked immunosorbent assay for zein and other proteins using unconventional solvents for antigen adsorptionAnalytical Biochemistry, 1984
- Influence of single amino acid substitutions on electrophoretic mobility of sodium dodecyl sulfate-protein complexesBiochemical and Biophysical Research Communications, 1978