spacer gif spacer gif spacer gif spacer gif spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    


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 Email this article to a friend
Right arrow Similar articles in this journal
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 LOVELESS, A.
Right arrow Articles by DANIELLI, J. F.
Right arrow Search for Related Content
PubMed
Right arrow Articles by LOVELESS, A.
Right arrow Articles by DANIELLI, J. F.

Quarterly Journal of Microscopical Science, Vol s3-90, 57-66, Copyright © 1949 by Company of Biologists

A Dye Phosphate for the Histo- and Cytochemical Demonstration of Alkaline Phosphatase, with some Observations on the Differential Behaviour of Nuclear and Extranuclear Enzymes

A. LOVELESS 1 and J. F. DANIELLI 1

1 Chester Beatty Research Institute, Royal Cancer Hospital, London, S.W. 3

1. A new method is described for the cyto- and histochemical demonstration of alkaline phosphatase (monoesterase), a synthetic substrate p-nitrobenzene-azo-4{alpha}-naphthol-phosphate being employed as the sodium salt. Two methods for preparing a solution of this substance are described, and optimal conditions for enzymic hydrolysis of the ester worked out by the use of kidney sections.

2. Experiments are also described in which the substrate has been used to demonstrate phosphatase activity in calcifying tissues of dogfish and rat.

3. The results of the experiments with rat kidney indicate that traces of end-products are necessary before the enzyme can attack this substrate.

4. When results obtained with the new substrate are compared with those obtained with {beta}-glycerophosphate, it is found that some sites display more activity towards one substrate than to the other.

5. The cytochemical localization of phosphatase with the new substrate is not as precise as with {beta}-glycerophosphate.







© The Company of Biologists Ltd 1949