Document Detail


Acid phosphatases of the rat epididymis. II. Biochemical characteristics, subcellular distribution and histochemical localization.
MedLine Citation:
PMID:  70177     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
After separation of three epididymal acid phosphatases their biochemical properties were differently studied. With appropriate substrate and inhibitor selection the distribution of the enzymes in different segments as well as the subcellular fractions of the rat epididymis was also demonstrated. The same biochemical differences were also utilized in the histochemical localization of the enzymes. It was found that Enzyme I had a pH-optimum at 5.0, a molecular weight of 97 000 and Km-constant of 0.901 mM. It was highly sensitive to tartrate and fluoride and it was localized in lysosomes as well as in the epididymal spermatozoa. Enzyme II had an optimum at pH 5.7, a molecular weight of 67 000 and Km-constant of 0.806 mM. It was also inhibited by fluoride but more resistant to tartrate. Its subcellular site was also particulate, but it was also found in the epididymal fluid. Enzyme III had an optimum at pH 5.2, a molecular weight of 135 000 and Km-constant of 0.685 m. It was resistant to low concentrations of fluoride and tartrate but sensitive to heavy metal ions. The enzyme was soluble and it behaved incoherently in thermal inactivation. All enzymes revealed the highest activity in the thin middle segments of the epididymis. Histochemical naphthol substrates gave a diffuse reaction in the epididymal epithelial cells. With the lead salt methods glycerophosphates and p-nitrophenylphosphate gave somewhat different results depending on their specificity as substrates for the epididymal enzymes. Both substrates gave a strong reaction supranuclearly in the Golgi area of the chief cells. This activity was inhibited by tartrate and was most probably due to Enzyme I. The epididymal corpus and cauda showed additionally a very strong apical activity in the chief cells with p-nitrophenylphosphate. This activity was resitant to tartrate but sensitive to fluoride. It was concluded that this enzyme represents Enzyme II activity. Similar activity was also found in the dissolving "holocrine" cells of the corpus and the cauda. The activity of the soluble Enzyme III could not be revealed with the present methods and the spermatozoa in the tubular lumina remained unstained.
Authors:
V Nikkanen; T Vanha-Perttula
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Andrologia     Volume:  9     ISSN:  0303-4569     ISO Abbreviation:  Andrologia     Publication Date:    1977 Apr-Jun
Date Detail:
Created Date:  1977-09-17     Completed Date:  1977-09-17     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0423506     Medline TA:  Andrologia     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  115-32     Citation Subset:  IM; S    
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MeSH Terms
Descriptor/Qualifier:
Acid Phosphatase / analysis*,  metabolism*
Animals
Epididymis / enzymology*
Fluorides / pharmacology
Glycerophosphates / pharmacology
Histocytochemistry
Hot Temperature
Hydrogen-Ion Concentration
Lysosomes / enzymology
Male
Molecular Weight
Naphthols / pharmacology
Rats
Spermatozoa / enzymology
Staining and Labeling
Subcellular Fractions / enzymology
Tartrates / pharmacology
Chemical
Reg. No./Substance:
0/Fluorides; 0/Glycerophosphates; 0/Naphthols; 0/Tartrates; EC 3.1.3.2/Acid Phosphatase

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


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