Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Plant Physiology 54:100-104 (1974)
© 1974 American Society of Plant Biologists

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 CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cerff, R.
Right arrow Articles by Quail, P. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cerff, R.
Right arrow Articles by Quail, P. H.
Agricola
Right arrow Articles by Cerff, R.
Right arrow Articles by Quail, P. H.
Articles

Glyceraldehyde 3-Phosphate Dehydrogenases and Glyoxylate Reductase

II. Far Red Light-Dependent Development of Glyceraldehyde 3-Phosphate Dehydrogenase Isozyme Activities in Sinapis Alba Cotyledons 1

R. Cerff and P. H. Quail2

a Biologisches Institut II, Universität Freiburg im Breisgau, 78 Freiburg, Schänzlestrasse 9-11, Germany

Ammonium sulfate chromatography has been employed to separate glyceraldehyde 3-phosphate dehydrogenases (GPD) of Sinapis alba cotyledons of various developmental stages. Cotyledons of dark-grown seedlings possess one major NAD-specific enzyme designated NAD-GPD I. Irradiation with continuous far red light leads to a strong increase in NADP-GPD activity and to the formation of a second NAD activity designated NAD-GPD II. These two activities occur in a constant ratio during cotyledon development, and they are eluted together in ammonium sulfate chromatography. In a later stage of cotyledon development the light-dependent increase in NAD-GPD II is matched by an equivalent decrease in NAD-GPD I. These data suggest that the chloroplast marker enzyme NADP-GPD (EC 1.2.1.13) also has NAD activity and that the light-dependent formation of this bifunctional enzyme is correlated with activity changes of the NAD-GPD of cytoplasmic glycolysis (EC 1.2.1.12).


2 Present address: Research School of Biological Sciences, The Australian National University, P.O. Box 475, Canberra City, A.C.T., Australia.

1 This work was financially supported by the Deutsche Forschungsgemeinschaft (SFB 46).







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1974 by the American Society of Plant Biologists