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 BERG, G. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by BERG, G. G.
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 STAINING OF TRIPHOSPHATASES BY THE CHELATE REMOVAL METHOD

GEORGE G. BERG 1

1 Department of Radiation Biology, The University of Rochester School of Medicine and Dentistry, Rochester, New York

In the histochemical staining of enzymes by the chelate removal method, the substrate is a chelate, and the enzyme unmasks bound ions which are precipitated by suitable capturing ions in the incubating mixture. The new method allows the staining of phosphatases which act on substrates that are insoluble in the Gomori mixtures.

Three inorganic polyphosphatases were stained in the first application of the chelate-removal principle: neutral triphosphatase, alkaline triphosphatase, and alkaline pyrophosphatase. The incubating media had lead-polyphosphate chelates as substrates, with "tris" or barbital buffers. Orthophosphate was added to some solutions as an auxiliary capturing anion.

Alkaline triphosphatase as well as alkaline pyrophosphatase was demonstrated in the columnar epithelium of duodenal mucosa of mouse and rat, alkaline triphosphatase in the convoluted tubules of kidney, and neutral triphosphatase in bile canaliculi of liver. The properties of the three enzymes were examined, and the relation of the stains to biochemically defined enzymes of the inorganic polyphosphatase group was discussed.

The chelate removal method was also used for the histochemical demonstration of adenosine tri- and diphosphatase. Evidence for this mechanism of ATP-ase staining is presented as an addendum.

Submitted on September 16, 1963


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 © 1964