Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Krishnan, H. B.
Right arrow Articles by White, J. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Krishnan, H. B.
Right arrow Articles by White, J. A.
Agricola
Right arrow Articles by Krishnan, H. B.
Right arrow Articles by White, J. A.

PLANT PHYSIOLOGY , Vol 109, Issue 4 1491-1495, Copyright © 1995 by American Society of Plant Biologists

RAPID COMMUNICATIONS

Morphometric Analysis of Rice Seed Protein Bodies (Implication for a Significant Contribution of Prolamine to the Total Protein Content of Rice Endosperm)

H. B. Krishnan and J. A. White
Department of Plant Pathology, University of Missouri, Columbia, Missouri 65211

Electron microscopic observation of thin sections of rice (Oryza sativa L.) endosperm revealed two types of protein bodies (PBs): spherical and irregular-shaped ones. Immunocytochemical localization studies using antibodies raised against purified glutelins, prolamines, and globulins indicated that the prolamines were localized in the spherical PB, whereas the irregular-shaped PB contained glutelins and globulins. We counted and measured the surface area and the relative volume of 2303 PBs randomly selected from two different developmental stages and from different locations within the endosperm. The ratio of spherical to irregular-shaped PBs was 1:1.6. Double-label immunogold electron microscopic localization indicated that the globulins represented about 18% of the surface area of the irregular-shaped PBs. Based on our morphometric analysis, we estimate the relative contribution of glutelin as 53%, that of prolamine as 35%, and that of globulin as 12% of the total seed protein.


This article has been cited by other articles:


Home page
 Plant Cell PhysiolHome page
F. Takaiwa, C. Sakuta, S.-K. Choi, Y. Tada, T. Motoyama, and S. Utsumi
Co-Expression of Soybean Glycinins A1aB1b and A3B4 Enhances Their Accumulation Levels in Transgenic Rice Seed
Plant Cell Physiol., October 1, 2008; 49(10): 1589 - 1599.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
Y. Kawagoe, K. Suzuki, M. Tasaki, H. Yasuda, K. Akagi, E. Katoh, N. K. Nishizawa, M. Ogawa, and F. Takaiwa
The Critical Role of Disulfide Bond Formation in Protein Sorting in the Endosperm of Rice
PLANT CELL, April 1, 2005; 17(4): 1141 - 1153.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1995 by the American Society of Plant Biologists