Skip Navigation

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 Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Lumsden, P. J.
Right arrow Articles by Furuva, M.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Lumsden, P. J.
Right arrow Articles by Furuva, M.
Agricola
Right arrow Articles by Lumsden, P. J.
Right arrow Articles by Furuva, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 1985, Vol. 26, No. 7 1313-1322
© 1985

Article

Effect of Monoclonal Antibodies on the in Vitro PFR Dark Reversion of Pea Phytochrome

Peter J. Lumsden, Kotaro T. Yamamoto, Akira Nagatani and Masaki Furuva1

Division of Biological Regulation, National Institute for Basic Biology Okazaki, Aichi 444, Japan

Extraction as PFR and immunoaffinity chromatography yielded a pea phytochrome sample with polypeptide size of 121 kdalton, the same as in a crude extract which was immediately heated in SDS. A difference spectrum was almost the same as that observed in etiolated pea epicotyls except that {delta}A666/{delta}A730 of 1.20 was significantly larger. At 10°C dark reversion from PFR occurred, with the decrease in A728 being almost equal to the increase in A667. The kinetics could be resolved into three first-order components, the major, slow component accounting for more than 90% of the absorbance changes. In the presence of monoclonal anti-pea phytochrome antibodies mAP-1, 3 or 5, which bind away from the chromophore, and mAP-7, which binds near the chromophore, the rate of the major component was reduced at either one or both wavelengths. None of these antibodies affected the absorption spectra of phytochrome. In the presence of mAP-9, which is suggested to bind near the amino-terminus, the absorption at the red-light-induced photostationary state was reduced and the rate of dark reversion was increased, resembling partially degraded phytochrome of 114 kdalton, but with no evidence of proteolysis.

1 Permanent address: Department of Botany, Faculty of Science, University of Tokyo, Hongo, Tokyo 113, Japan.

(Received June 15, 1985; Accepted July 30, 1985)
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Plant CellHome page
A. Hisada, H. Hanzawa, J. L. Weller, A. Nagatani, J. B. Reid, and M. Furuya
Light-Induced Nuclear Translocation of Endogenous Pea Phytochrome A Visualized by Immunocytochemical Procedures
PLANT CELL, July 1, 2000; 12(7): 1063 - 1078.
[Abstract] [Full Text]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.