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 KALINA, M.
Right arrow Articles by PEARSE, A. G. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by KALINA, M.
Right arrow Articles by PEARSE, A. G. 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?

ULTRASTRUCTURAL LOCALIZATION OF SUCCINATE DEHYDROGENASE IN MOUSE LIVER MITOCHONDRIA; A CYTOCHEMICAL STUDY

MOSHE KALINA 1, BARRY WEAVERS 1, and A. G. E. PEARSE 1

1 Department of Cell Biology and Histology, Tel Aviv University Medical School, Tel Aviv, Israel, and Department of Histochemistry, Royal Postgraduate Medical School, London, England

Ultrastructural localization of succinate dehydrogenase, employed as a marker of the electron transfer chain, was studied in mouse liver mitochondria either in orthodox or condensed conformation. Activity of succinate dehydrogenase in the orthodox form mitochondria was localized primarily on the cristal membrane facing the matrix. A prolonged incubation time resulted in reaction product filling the intracristal space, whereas a short incubation time resulted also in a product which appeared mainly at opposite points on both sides of the crista. No such arrangement of the reaction product was noted in mitochondria in the condensed conformation. These findings, supported by studies of serial sections, suggest that the reaction product in orthodox form mitochondria appears in bands or coils surrounding the whole cristal membrane.

Submitted on November 29, 1969


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
 Biol. Reprod.Home page
F. M. Flesch, W. F. Voorhout, B. Colenbrander, L. M.G. van Golde, and B. M. Gadella
Use of Lectins to Characterize Plasma Membrane Preparations from Boar Spermatozoa: A Novel Technique for Monitoring Membrane Purity and Quantity
Biol Reprod, December 1, 1998; 59(6): 1530 - 1539.
[Abstract] [Full Text]



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