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


     

Plant Physiology 77:695-699 (1985)
© 1985 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 Web of Science
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 Web of Science (17)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by de Ruiter, H.
Right arrow Articles by Kollöffel, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by de Ruiter, H.
Right arrow Articles by Kollöffel, C.
Agricola
Right arrow Articles by de Ruiter, H.
Right arrow Articles by Kollöffel, C.
Articles

Properties of Ornithine Carbamoyltransferase from Pisum sativum L

Hans de Ruiter and Chris Kollöffel

Botanical Laboratory, University of Utrecht, Utrecht, The Netherlands

Some properties of ornithine carbamoyltransferase from chloroplasts isolated from leaves of Pisum sativum L. (cv Marzia) were compared with those of the enzyme partially purified (316-fold) from shoots of seedlings after 3 weeks of cultivation.

Both preparations showed a pH optimum at pH 8.3 and had the same affinity to ornithine (Km = 1.2 millimolar) as well as to carbamoyl phosphate (Km = 0.2 millimolar). The approximate molecular weight determined by gel sieving was 77,600.

A desalted ammonium sulfate precipitate from 14-day seedlings (inclusive roots and senescing cotyledons) was applied on a column of anion exchanger. The elution pattern showed one peak of ornithine carbamoyl-transferase activity. This elution pattern was the same as observed for the enzyme from chloroplasts.

The results suggest the presence of one form of ornithine carbamoyl-transferase in pea seedlings.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1985 by the American Society of Plant Biologists