Literature DB >> 6294006

The cytochemical demonstration of NaK dependent adenosine triphosphatase at electrocyte level in Eigenmannia virescens (Gymnotidae).

J P Denizot.   

Abstract

ATPase activity (E.C. 3.6.1.3.) has been studied by electron microscopy with the help of several cytochemical techniques on Eigenmannia virescens electrocytes. Incubation was carried out with in two different media containing paranitrophenyl phosphate (p-NPP) or adenosine triphosphate (ATP) as substrate. With p-NPP the phosphate freed is captured at alkaline pH, either by strontium chloride or by lead citrate. With ATP the phosphate freed is captured at a pH close to neutrality by the lead nitrate. NaK ATPase activity was only demonstrated with the medium containing ATP; the positive results obtained with this technique were sensitive to ouabain. The enzyme is situated both on the membrane of the posterior face which is innervated and on that of the anterior face of the electrocytes. The cytoplasm of the anterior face is occupied by a strong concentration of tubules on whose membranes the enzyme is also present. The localisation of the enzyme on the tubules can explain biochemical results which indicate that 70% of the total NaK ATPase of the electrolytes is situated at the level of the anterior face.

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Year:  1982        PMID: 6294006     DOI: 10.1007/bf00495831

Source DB:  PubMed          Journal:  Histochemistry        ISSN: 0301-5564


  21 in total

1.  Ion movements studied with single isolated electroplax.

Authors:  E SCHOFFENIELS
Journal:  Ann N Y Acad Sci       Date:  1959-08-28       Impact factor: 5.691

2.  Distribution of histochemically demonstrable sodium and potassium activated adenosine triphosphatase in the rat lens with comments on methodology.

Authors:  M Palva; T Tervo; A Palkama
Journal:  Cell Mol Biol Incl Cyto Enzymol       Date:  1978

3.  Sodium-potassium-activated adenosine triphosphatase. VII. Concurrent inhibition of NA + -K + -adenosine triphosphatase and activation K + -nitrophenylphosphatase activities.

Authors:  R W Albers; G J Koval
Journal:  J Biol Chem       Date:  1972-05-25       Impact factor: 5.157

4.  Transport adenosine triphosphatase cytochemistry. II. Cytochemical localization of ouabin-sensitive, potassium-dependent phosphatase activity in the secretory epithelium of the avian salt gland.

Authors:  S A Ernst
Journal:  J Histochem Cytochem       Date:  1972-01       Impact factor: 2.479

5.  Sodium-potassium-activated adenosine triphosphatase of Electrophorus electric organ. I. An associated sodium-activated transphosphorylation.

Authors:  S Fahn; G J Koval; R W Albers
Journal:  J Biol Chem       Date:  1966-04-25       Impact factor: 5.157

6.  Histochemical demonstration of (Na+-K+)-activated adenosine triphosphatase.

Authors:  L Guth; R W Albers
Journal:  J Histochem Cytochem       Date:  1974-05       Impact factor: 2.479

7.  A quantitative biochemical and histochemical study of the lead method for localization of adenosine triphosphate-hydrolyzing enzymes.

Authors:  N O Jacobsen; P L Jorgensen
Journal:  J Histochem Cytochem       Date:  1969-07       Impact factor: 2.479

8.  Adenosine triphosphatases in electroreceptor organs (ampullary organs and mormyromasts) of Gnathonemus petersii Mormyridae.

Authors:  J P Denizot
Journal:  Histochem J       Date:  1982-03

9.  A new one-step method for the cytochemical localization of ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase activity.

Authors:  H Mayahara; K Fujimoto; T Ando; K Ogawa
Journal:  Histochemistry       Date:  1980

10.  Transport ATPase cytochemistry: ultrastructural localization of potassium-dependent and potassium-independent phosphatase activities in rat kidney cortex.

Authors:  S A Ernst
Journal:  J Cell Biol       Date:  1975-09       Impact factor: 10.539

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  2 in total

1.  A highly polarized excitable cell separates sodium channels from sodium-activated potassium channels by more than a millimeter.

Authors:  Yue Ban; Benjamin E Smith; Michael R Markham
Journal:  J Neurophysiol       Date:  2015-04-29       Impact factor: 2.714

2.  Ultrastructural demonstration of alkaline phosphatase (ALP) and K+-p-nitrophenyl phosphatase (K+-p-NPPase) in the epidermal ionocytes of Blennius sanguinolentus.

Authors:  G Zaccone; S Fasulo; A Licata
Journal:  Histochemistry       Date:  1984
  2 in total

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