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


     

Plant Physiology 61:663-666 (1978)
© 1978 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 HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (42)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wong, K. F.
Right arrow Articles by Craigie, J. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wong, K. F.
Right arrow Articles by Craigie, J. S.
Agricola
Right arrow Articles by Wong, K. F.
Right arrow Articles by Craigie, J. S.
Articles

Sulfohydrolase Activity and Carrageenan Biosynthesis in Chondrus crispus (Rhodophyceae) 1

Kwan F. Wong and James S. Craigie

Atlantic Regional Laboratory, National Research Council of Canada, Halifax, Nova Scotia B3H 3Z1

An enzyme catalyzing the conversion of µ- to {kappa}-carrageenan has been demonstrated in both haploid and diploid plants of Chondrus crispus. It acts at the polymer level producing 3,6-anhydro-D-galactose with the stoichiometric release of sulfate. Two-thirds of the recoverable enzyme was associated with the 15,000g pellet most of which could be solubilized by passage through a Ribi Cell Fractionator. The enzyme precipitated between 2.65 and 4.24 M (NH4)2SO4 and was partly purified on DEAE-cellulose columns. This sulfohydrolase has a pH optimum near 6.5 and is inhibited by molybdate, phosphate, sulfate, tungstate, cysteine, ATP, GTP, UDP, and by {lambda}-carrageenan. No activator was found. The enzyme showed a similar affinity for several preparations of µ-carrageenan and for the {kappa}-carrageenase-resistant fraction from {kappa}-carrageenan thus confirming that the latter is a biosynthetically unfinished molecule.

A comparable extract from Gigartina stellata gave a higher specific activity for the sulfohydrolase, but was otherwise quite similar to the Chondrus enzyme.

1 Issued as NRCC No. 16473.




This article has been cited by other articles:


Home page
 Plant Physiol.Home page
S. Genicot-Joncour, A. Poinas, O. Richard, P. Potin, B. Rudolph, B. Kloareg, and W. Helbert
The Cyclization of the 3,6-Anhydro-Galactose Ring of {iota}-Carrageenan Is Catalyzed by Two D-Galactose-2,6-Sulfurylases in the Red Alga Chondrus crispus
Plant Physiology, November 1, 2009; 151(3): 1609 - 1616.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1978 by the American Society of Plant Biologists