Structure of maize protein bodies and immunocytochemical localization of zeins |
| |
Authors: | C R Lending A L Kriz B A Larkins C E Bracker |
| |
Institution: | (1) Department of Agronomy, University of Illinois, 61801 Urbana, IL, USA;(2) Department of Botany and Plant Pathology, Purdue University, 47907 West Lafayette, IN, USA |
| |
Abstract: | Summary Zeins, the seed storage proteins of maize (Zea mays L.), are synthesized by membrane-bound polyribosomes and transported into the lumen of the endoplasmic reticulum in developing endosperm, where they assemble into protein bodies. To better understand the organization of protein bodies and the mechanism by which zeins are assembled, we have used immunolocalization to study their distribution within isolated protein bodies. In sections stained with uranyl acetate and lead citrate, the protein body matrix consists of light- and dark-staining regions with the darker stain predominating at the periphery and the lighter stain in the central region. Immunogold staining of the storage proteins in isolated protein bodies reveals a distinct segregation with -zein localized in the light-staining region and - and -zein localized in the dark-staining regions. However, the relative amounts and distribution of these proteins varies substantially among different protein bodies. These results indicate a more complex internal organization than has been previously observed, and suggest that spatial and/or temporal differences in zein synthesis account for this complexity.Abbreviations BSA
bovine serum albumin
- IgG
immunoglobulin G
- PB
phosphate buffer
- SDS
sodium dodecyl sulfate
- SDS-PAGE
sodium dodecyl sulfate-polyacrylamide gel electrophoresis
- TTBS
Tween-20/tris-buffered saline
- TBS-T
Tris-buffered saline/Tween-20
- TBS-T-B
Tris-buffered saline/Tween-20/bovine serum albumin |
| |
Keywords: | Immunolocalization Zein Protein bodies Zea mays Rough endoplasmic reticulum |
本文献已被 SpringerLink 等数据库收录! |
|