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


     


Plant Physiology 59:925-929 (1977)
© 1977 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 Ewing, E. E.
Right arrow Articles by Hedges, A. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ewing, E. E.
Right arrow Articles by Hedges, A. M.
Agricola
Right arrow Articles by Ewing, E. E.
Right arrow Articles by Hedges, A. M.
Articles

Changes in Potato Tuber Invertase and Its Endogenous Inhibitor After Slicing, Including a Study of Assay Methods 1,2

Elmer E. Ewing, Maria Devlin3, Deborah A. McNeill4, Martha H. McAdoo5 and Anne M. Hedges

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

The increase in the invertase activity of extracts from freshly cut potato (Solanum tuberosum L.) by "foaming," caused by selective denaturation of an endogenous invertase inhibitor, did not occur in extracts made from thin disks 2 days after slicing. Rather, foaming such extracts decreased invertase activity. Apparently, the inhibitor disappeared after slicing, and the enzyme became more labile to foaming. Such disappearance of inhibitor could account for up to 15% of the dramatic increase in total invertase activity that had occurred within 2 days after slicing. The difference between extracts from 0-day and 2-day slices was mainly in the first of two peaks of invertase activity eluted from diethylaminoethyl-cellulose columns. This peak was increased by foaming 0-day extracts, but even when foamed was much smaller than in 2-day extracts. The apparent loss in inhibitor was not caused by a decreasing susceptibility of the enzyme to the inhibitor. Both the increase in total invertase activity and the apparent loss of inhibitor after slicing were partially blocked by actinomycin D and completely blocked by cycloheximide.

The presence of the inhibitor can lead to serious errors in the usual whole disk method of assay for invertase in slices. Ethyl acetate treatment reduces the solubility of the enzyme but does not inactivate the inhibitor.


3 Present address: Department of Immunology, Rush-Presbyterian-St. Luke's Medical Center, Chicago, Ill. 60612.

4 Present address: 1613 E. Genesee St., Syracuse, N. Y. 13201.

5 Present address: 62 Le Brun Court, Galveston, Tex. 77550.

1 Supported by Hatch funds granted to Cornell University.

2 Paper 678 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 © 1977 by the American Society of Plant Biologists