Document Detail

The cytochemical demonstration of prostatic acid phosphatase using a new substrate, phosphorylcholine.
MedLine Citation:
PMID:  977936     Owner:  NLM     Status:  MEDLINE    
Prostatic acid phosphatase (PAP), an acid phosphatase specific to the prostate gland, is demonstrated cytochemically for both light and electron microscopy with a new substrate phosphorylcholine. Lead ion is used as capture agent for liberated phosphate ion in a modified Gomori medium. PAP is demonstrated in the tubuloaveolar epithelial secretory cells of the rat ventral prostate gland. In the apical portion of the cell it is found in secretory granules and in the matrix of multivescular bodies. In the Golgi area it is localized in Golgi cisternae, Golgi related vacuoles and multivescular bodies. Evidence is presented that PAP is not a lysosomal enzyme, as are other acid phosphatases, and that phosphorylcholine is a highly specific substrate for PAP. As based on the role of pentavalent nitrogen on substrate structure, it is apparent that PAP is to other acid phosphatases what the cholinesterases are to other esterases.
J A Serrano; W A Shannon; N J Sternberger; H L Wasserkrug; A A Serrano; A M Seligman
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society     Volume:  24     ISSN:  0022-1554     ISO Abbreviation:  J. Histochem. Cytochem.     Publication Date:  1976 Oct 
Date Detail:
Created Date:  1976-12-30     Completed Date:  1976-12-30     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9815334     Medline TA:  J Histochem Cytochem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1046-56     Citation Subset:  IM    
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MeSH Terms
Acid Phosphatase / metabolism*
Choline* / analogs & derivatives
Epithelial Cells
Epithelium / enzymology,  ultrastructure
Microscopy, Electron
Prostate / enzymology*,  ultrastructure
Reg. No./Substance:
107-73-3/Phosphorylcholine; 62-49-7/Choline; EC Phosphatase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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