Journal of Histochemistry and Cytochemistry Priciples for Free Access to Science
  Search:   
    >> Advanced Search

Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
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 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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by GOLDFISCHER, S.
Right arrow Articles by ESSNER, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by GOLDFISCHER, S.
Right arrow Articles by ESSNER, E.
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?

NUCLEOSIDE DIPHOSPHATASE AND THIAMINE PYROPHOSPHATASE ACTIVITIES IN THE ENDOPLASMIC RETICULUM AND GOLGI APPARATUS

SIDNEY GOLDFISCHER 1, BERNICE SCHILLER 1, and EDWARD ESSNER 2

1 Department of Pathology, Albert Einstein College of Medicine, Bronx, New York 10461
2 Division of Cytology, Sloan Kettering Institute, New York, New York 10021

The effects of pH, fixatives and divalent ions on nucleoside diphosphatase (NDPase) and thiamine pyrophosphatase (TPPase) activities in the endoplasmic reticulum (ER) and Golgi apparatus (GA) were examined in adult and neonatal hepatocytes and other cell types in the rat. In liver cells TPPase and NDPase both have a similar localization in the rough ER, nuclear envelope and smooth ER but differ in their pH optima; TPPase is most active at pH 8, NDPase at pH 7. TPPase in the GA, unlike its counterpart in the ER, is most active at neutral pH. High levels of NDPase activity are present in the GA of neurons, epididymis and other cells, but not in hepatocytes. TPPase in the ER, but not the GA, is stimulated by the addition of adenosine triphosphate to the medium. These observations show that different conditions are required to demonstrate ER and GA diphosphatase activities. Whether separate enzymes or multiple configurations of a single protein are responsible for these activities cannot be determined by staining procedures.

Submitted on February 17, 1971


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?


This article has been cited by other articles:


Home page
 FASEB J.Home page
E. Errasti-Murugarren, M. Molina-Arcas, F. J. Casado, and M. Pastor-Anglada
A splice variant of the SLC28A3 gene encodes a novel human concentrative nucleoside transporter-3 (hCNT3) protein localized in the endoplasmic reticulum
FASEB J, January 1, 2009; 23(1): 172 - 182.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. L. Swift and L. L. Swift
Role of the Golgi Apparatus in the Phosphorylation of Apolipoprotein B
J. Biol. Chem., December 6, 1996; 271(49): 31491 - 31495.
[Abstract] [Full Text] [PDF]



Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
The Journal of Histochemistry & Cytochemistry is owned, published, and licensed by The Histochemical Society © 1971