scholarly journals Cytochemical Localization of ATPase Activity in Oat Roots Localizes a Plasma Membrane-Associated Soluble Phosphatase, Not the Proton Pump

1988 ◽  
Vol 86 (3) ◽  
pp. 841-847 ◽  
Author(s):  
Donald B. Katz ◽  
Michael R. Sussman ◽  
Robert J. Mierzwa ◽  
Ray F. Evert
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Proton Pump ◽  
Cytochemical Localization

scholarly journals Cytochemical localization of ecto-ATPases in rat neurohypophysis.

1996 ◽  
Vol 44 (2) ◽  
pp. 103-111 ◽  
Author(s):  
S Thirion ◽  
J D Troadec ◽  
G Nicaise
Keyword(s):  
Electron Microscopy ◽  
Plasma Membrane ◽  
Atpase Activity ◽  
Outer Surface ◽  
Nerve Endings ◽  
Glutaraldehyde Fixation ◽  
Cytochemical Localization ◽  
Cytochemical Method ◽  
Ca Pump ◽  
Dependent Atpase

We studied the distribution of Ca(2+)- or Mg(2+)-dependent ATPase activity in rat neurohypophysis using the lead cytochemical method of Ando et al. In electron microscopy, precipitates were found lining the outer surface of the plasma membrane surrounding nerve endings and pituicytes. These precipitates were believed to represent the activity of ecto-ATPases (as opposed to Ca pump ATPases) for the following reasons: there was equal activation by Ca2+ in the absence of Mg2+ or Mg2+ in the absence of Ca2+; the effects of the two ions were not additive; there was activation by ATP or GTP; and there was resistance to glutaraldehyde fixation, to high (10 mM) Ca2+ concentrations, and to various inhibitors such as NEM, vanadate, oligomycin, quercetin, p-chloromercuribenzoate, ouabain, and levamisole. Cytosolic activity observed in certain nerve endings in the same conditions of incubation but more sensitive to NEM is also described and discussed.

scholarly journals Cytochemical localization of ouabain-sensitive (K+)-dependent p-nitrophenyl phosphatase (transport ATPase) in human blood platelets.

1980 ◽  
Vol 28 (11) ◽  
pp. 1183-1188 ◽  
Author(s):  
L S Cutler ◽  
M B Feinstein ◽  
C P Christian
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Human Blood ◽  
Human Platelet ◽  
Blood Platelets ◽  
Cytochemical Localization ◽  
Transport Atpase ◽  
Tubular System ◽  
Membrane Compartments ◽  
Human Blood Platelets

The ultrastructural cytochemical localization of a potassium-dependent oubain-sensitive nitrophenyl phosphatase (transport ATPase) activity in human blood platelets is described. This potassium-dependent nitrophenyl phosphatase activity was not affected by 5 mM levamisole, indicating that the reaction product identified was not due to nonspecific alkaline phosphatase activity. The K+-dependent nitrophenyl phosphatase was strictly localized to the platelet plasma membrane, while the open canalicular system and dense tubular system were devoid of reaction product. In contrast, (Ca2+,Mg2+)-activated ATPase activity was predominantly localized in the open canalicular system and dense tubular system with very little cytochemical activity expressed at the plasma membrane. These data demonstrate a relative segregation of these enzymes into unique membrane compartments of the human platelet. Such data may be useful with regard to identification of purified membrane fractions from platelets and may be significant with regard to the understanding of the function(s) of the different membrane compartments of the human platelet.

Cytochemical localization of plasma membrane ATPase activity in plant cells

PROTOPLASMA ◽  
1991 ◽  
Vol 165 (1-3) ◽  
pp. 27-36 ◽  
Author(s):  
E. Chauhan ◽  
D. S. Cowan ◽  
J. L. Hall
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Plant Cells ◽  
Plasma Membrane Atpase ◽  
Cytochemical Localization ◽  
Membrane Atpase

Localization of Adenosine Triphosphatase Activity in the Phleom of Nicotiana Tabacum

1972 ◽  
Vol 30 ◽  
pp. 230-231
Author(s):  
James Cronshaw ◽  
Jamison E. Gilder
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Higher Plants ◽  
High Surface ◽  
Root Tip ◽  
Animal Cells ◽  
Physiological Processes ◽  
Tip Cells ◽  
Atpase Localization

Adenosine triphosphatase (ATPase) activity has been shown to be associated with numerous physiological processes in both plants and animal cells. Biochemical studies have shown that in higher plants ATPase activity is high in cell wall preparations and is associated with the plasma membrane, nuclei, mitochondria, chloroplasts and lysosomes. However, there have been only a few ATPase localization studies of higher plants at the electron microscope level. Poux (1967) demonstrated ATPase activity associated with most cellular organelles in the protoderm cells of Cucumis roots. Hall (1971) has demonstrated ATPase activity in root tip cells of Zea mays. There was high surface activity largely associated with the plasma membrane and plasmodesmata. ATPase activity was also demonstrated in mitochondria, dictyosomes, endoplasmic reticulum and plastids.

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