The use of two‐dimensional gel electrophoresis in the analysis of organ‐specific maize proteins
- 1 January 1988
- journal article
- research article
- Published by Wiley in Electrophoresis
- Vol. 9 (11) , 738-741
- https://doi.org/10.1002/elps.1150091109
Abstract
Two‐dimensional gel electrophoresis with non‐equilibrium pH gradient electrophoresis in the first dimension and sodium dodecyl sulfate‐polyacrylamide gels in the second dimension has been used for the analysis of organ‐specific proteins in maize. The method has been used to study the whole protein pattern of developing organs and adult leaves as well as protein patterns of in vitro translation. Examples of two‐dimensional immunoblotting and in vitro translation of endosperm‐specific proteins are also shown. Two‐dimensional gel electrophoresis appears as an essential analytical step in the identification of organ‐specific proteins and for the detection of the protein products related to organ‐specific genes identified by other means.This publication has 15 references indexed in Scilit:
- Regulation of Gene Expression in Developing Zea mays EmbryosPlant Physiology, 1986
- Immunological relations between glutelin-2 and low molecular weight zein-2 proteins from maize (Zea Mays L) endospermPlant Science, 1985
- Two-dimensional gel electrophoresis of zein proteins from normal and opaque-2 maize with non-ionic detergent acid urea-polyacrylamide gel electrophoresis in the first dimensionPlant Science Letters, 1984
- Hormonal Control of Mitotic Development in Tobacco ProtoplastsPlant Physiology, 1981
- Silver staining of proteins in polyacrylamide gelsAnalytical Biochemistry, 1981
- High resolution two-dimensional electrophoresis of basic as well as acidic proteinsCell, 1977
- Storage Protein Synthesis in MaizePlant Physiology, 1976
- Assay of proteins in the presence of interfering materialsAnalytical Biochemistry, 1976
- [63] Rapid isolation techniques for chloroplastsPublished by Elsevier ,1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970