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


     

Plant Physiology 66:451-456 (1980)
© 1980 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 (12)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Anderson, R. S.
Right arrow Articles by Senesac, A. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Anderson, R. S.
Right arrow Articles by Senesac, A. H.
Agricola
Right arrow Articles by Anderson, R. S.
Right arrow Articles by Senesac, A. H.
Articles

Inhibition of Potato Tuber Invertase by an Endogenous Inhibitor

EFFECTS OF SALTS, pH, TEMPERATURE, AND SUGARS ON BINDING 1, ,2

Roger S. Anderson3, Elmer E. Ewing4 and Anne Hedges Senesac

Department of Vegetable Crops, Cornell University, Ithaca, New York 14853

Binding between potato tuber invertase and its endogenous inhibitor followed second-order reaction kinetics. Binding rates were diminished by the presence of various inorganic salts, MgCl2 being especially effective. This effect of MgCl2 was used in binding rate studies by adding the salt with sucrose to reduce binding during assay of previously unbound activity. The optimal pH for binding was about 4.8, similar to the optimal pH for catalytic activity of invertase. The optimal temperature for binding was about 45 C, approximately 5 C less than the optimum for catalytic activity. Sucrose at concentrations as low as 2 millimolar slowed binding; reducing sugars had little or no effect on binding or on catalytic activity.

3 Present address: Department of Nutrition and Food Science, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139.

4 To whom reprint requests should be addressed.

1 The major portion of this paper constitutes part of a Ph.D. thesis presented to Cornell University by R. S. A., the recipient of a Liberty Hyde Bailey Fellowship from the Department of Vegetable Crops. The work was also supported by Hatch Regional Marketing Funds granted to the Department of Vegetable Crops.

2 This is Paper No. 755 of the Department of Vegetable Crops, Cornell University.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1980 by the American Society of Plant Biologists