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 LAZARUS, S. S.
Right arrow Articles by WALLACE, B. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by LAZARUS, S. S.
Right arrow Articles by WALLACE, B. J.
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 PHOSPHATASE AND THIAMINE PYROPHOSPHATASE ACTIVITY OF RABBIT GOLGI APPARATUS

SYDNEY S. LAZARUS 1 and BARBARA J. WALLACE 1

1 Isaac Albert Research Institute of the Jewish Chronic Disease Hospital, Brookyln, New York

The Golgi associated nucleoside phosphatase which is demonstrable in rabbit pancreatic islet cells at alkaline pH using briefly postfixed cryostat sections and a modified Padykula-Herman incubation solution rapidly hydrolyzes uridine triphosphate (UTP) as well as uridine (UDP) and inosine diphosphate (IDP), but not thiamine pyrophosphate (TPP). Staining in the Golgi apparatus of islet cells was markedly attenuated when a lead incubation solution was employed at pH 7.2 with these same nucleoside-phosphates as substrates. The enzyme was not demonstrable in sections cut from tissue blocks fixed for 24 hours in formalin. This enzyme was distributed in the Golgi apparatus of some cellular elements of many other rabbit tissues. In rabbit cortical neurons a different Golgi enzyme was demonstrated which at alkaline pH hydrolyzed TPP but not UTP, IDP or UDP. This enzyme was also demonstrable with the lead method at pH 7.2 and under these conditions hydrolyzed IDP and UDP as well as TPP, but not UTP. The neuronal enzymatic activity was much less formalin-sensitive than that in pancreatic islet Golgi apparatus surviving in 24-hr formalin-fixed tissue blocks. This latter enzyme could be demonstrated in addition to brain only in the Golgi apparatus of hypophysis and epididymis. Differences in substrate specificity and of response to adjuvants as well as the differences in distribution confirm that these are two distinct enzymes.

Submitted on February 24, 1964
Revised on August 13, 1964


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