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 Google Scholar
Google Scholar
Right arrow Articles by Revis, N. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Revis, N. 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?

Localization of adenylate cyclase in unfixed sections of cardiac muscle

NW Revis

Previous investigators have shown that prefixation and lead staining completely inhibit the activity of adenylate cyclase. Lead has also been shown to stimulate the nonenzymatic hydrolysis of AMP-PMP (the substrate for adenylate cyclase) after 30 min incubation. The present studies were performed to determine if the omission of prefixation would provide a better method for localizing adenylate cyclase in cardiac muscle. These studies were also performed to determine the effect of short incubation on the lead-induced nonenzymatic hydrolysis of AMP-PNP. In prefixed sections the reaction product was diffusely localized over the section. However, in unfixed sections the reaction product appeared only on the sarcolemma and sarcotubule system. Results are presented showing that short incubation (i.e., 5 min) prevents the nonenzymatic hydrolysis of AMP-PMP by lead. In biochemical studies lead (10(-3) M) was shown to completely inhibit the activity of this enzyme. However, in the presence of 4 micrograms phosphatidylinositol, lead inhibition of this enzyme was reduced to 50% of the control value. Based on this observation, it is suggested that approximately 50% of adenylate cyclase is present in sections of cardiac muscle exposed to 2 x 10(-3) M lead, which is presumably enough activity for demonstration of adenylate cyclase activity.

Volume 27, Issue 10, pp. 1322-1326, 10/01/1979
Copyright © 1979 by The Histochemical Society


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?





Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
The Journal of Histochemistry & Cytochemistry is owned, published, and licensed by The Histochemical Society © 1979