The Journal of General Physiology
VISIT JCB ONLINE!
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article
Right arrow Full Text (PDF, 833K)
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JGP
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kaplan, J. G.
Right arrow Articles by Tacreiter, W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kaplan, J. G.
Right arrow Articles by Tacreiter, W.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
The Journal of General Physiology, Vol 50, 9-24, Copyright © 1966 by The Rockefeller University Press


ARTICLE

The ß-Glucosidase of the Yeast Cell Surface

J. Gordin Kaplan 1 and Wanda Tacreiter 1

1 From the Department of Physiology and Biophysics, Dalhousie University, Halifax, Nova Scotia, Canada.

Dr. Kaplan's present address is the Department of Biology, The University of Ottawa, Canada

There are two distinct components of the system which limits the rate at which intact cells of S. cerevisiae C hydrolyze external ß-glucosides; one component requires metabolic energy and the other is stereospecific for ß-glucosides. The stereospecific component is localized at the cell membrane, as shown by its sensitivity to heavy metal inhibitors which did not penetrate the cell under the conditions used. It was shown that cellobiose-grown cells were able to remove cellobiose from the medium in which they were incubated, and that the cellobiose uptake system was identical to that which limits the patent ß-glucosidase activity. In order to test the hypothesis that the system in question was a transport system, for ß-glucosides the ability of cellobiose-grown cells to take up 14C-labeled methyl-ß-glucoside (MBG) was studied. The induced cells were able to take up MBG-14C and the label could be partially chased out by cold MBG and cellobiose; glucose-grown cells could not incorporate label. However, induced cells could not take up label when incubated with 14C-MBG, thus excluding the hypothesis of transport of intact ß-glucosides. It was concluded that the stereospecific membrane component was actually a ß-glucosidase, coupled to an energy-dependent transport system for the glucose moiety; the function of the latter was rate-limiting in the over-all activity of the entire system.

Submitted on December 9, 1965


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?




  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents