adenosine triphosphatases

2020 ◽  
Author(s):  
D.A. Thayer
Keyword(s):  
Adenosine Triphosphatases

Inhibition of Adenosine Triphosphatases in Vitro by Silver Nitrate and Silver Sulfadiazine

1984 ◽  
Vol 3 (1) ◽  
pp. 37-42 ◽  
Author(s):  
B. R. Nechay ◽  
J. P. Saunders
Keyword(s):  
Silver Nitrate ◽  
Aqueous Suspension ◽  
Human Kidney ◽  
Silver Sulfadiazine ◽  
Constant Concentration ◽  
Inhibitory Potency ◽  
Adenosine Triphosphatases ◽  
Tissue Homogenates ◽  
Atpase Inhibition

Inhibition of adenosine triphosphatase (ATPase) by silver nitrate (AgNO3) in vitro was studied in microsomal fractions or tissue homogenates of canine brain and kidney and human kidney. In microsomal fractions, AgNO3 was an indiscriminate inhibitor of ouabain-sensitive (Na+ + K+ ATPase) and ouabain-insensitive (Mg2+ ATPase) activities, with 50% inhibition obtaining at concentrations on the order of 10–7 to 10–6 M. Changing the concentrations of Na+, K+, H+, Mg2+, and ATP did not alter the fractional inhibition of Na+ + K+ ATPase by a constant concentration of AgNO3. An aqueous suspension of silver sulfadiazine had an inhibitory potency similar to AgNO3. It was concluded that silver gives a different pattern of Na+ + K+ ATPase inhibition than other metallic inhibitors of the enzyme so far examined.

scholarly journals Characterization of cuckoo-pint (Arum maculatum) mitochondrial adenosine triphosphatases

1986 ◽  
Vol 233 (3) ◽  
pp. 839-844 ◽  
Author(s):  
P P J Dunn ◽  
A R Slabas ◽  
A L Moore
Keyword(s):  
Adenosine Triphosphatase ◽  
Kinetic Properties ◽  
Ph Profile ◽  
Enzyme Preparations ◽  
Adenosine Triphosphatases ◽  
Membrane Bound ◽  
Cold Stability ◽  
Arum Maculatum ◽  
Guanosine Triphosphatase ◽  
Soluble Enzymes

The catalytic properties of cuckoo-pint (Arum maculatum) mitochondrial adenosine triphosphatase have been analysed. The pH profile, effect of inhibitors, cold-stability and substrate specificity are characteristic of mitochondrial adenosine triphosphatases, although a high guanosine triphosphatase activity does appear to be restricted to plant mitochondrial adenosine triphosphatases. The kinetic properties of nucleoside 5′-triphosphate hydrolysis by membrane-bound and soluble enzymes have been studied by means of double-reciprocal plots. These plots were linear in the absence of an activating anion, which may indicate that the catalytic and/or regulatory mechanism of Arum maculatum adenosine triphosphatase is different from that of other enzyme preparations. It is suggested that the differences in subunit composition of plant and mammalian adenosine triphosphatases reported previously [Dunn, Slabas & Moore (1985) Biochem. J. 225, 821-824] are structurally, rather than functionally, significant.

Transport adenosine triphosphatases: properties and functions.

1981 ◽  
Vol 61 (1) ◽  
pp. 1-76 ◽  
Author(s):  
F Schuurmans Stekhoven ◽  
S L Bonting
Keyword(s):  
Adenosine Triphosphatases

scholarly journals Salt-Stimulated Adenosine Triphosphatases from Carrot, Beet, and Chara Australis

1967 ◽  
Vol 20 (6) ◽  
pp. 1069 ◽  
Author(s):  
MR Atkinson ◽  
GM Polya
Keyword(s):  
Fresh Water ◽  
Choline Chloride ◽  
Potassium Sulphate ◽  
Adenosine Triphosphatases ◽  
Chara Australis ◽  
Transport Atpases ◽  
Fresh Water Alga ◽  
Sodium And Potassium ◽  
Animal Transport

Soluble adenosine triphosphatases (ATPases) from carrot, beetroot, and the fresh-water alga Ohara australi8 were activated by sodium and potassium chlorides, but not by choline chloride, and were inhibited by potassium sulphate and fluoride. Ouabain was not inhibitory, and Na+-K+ synergism of the type found with animal "transport" ATPases was not observed.

Oscillatory Activity of P-Type Membrane Adenosine Triphosphatases: a Kinetic Model

2005 ◽  
Vol 70 (4) ◽  
pp. 440-444 ◽  
Author(s):  
B. N. Goldstein ◽  
A. A. Mayevsky ◽  
D. T. Zakrjevskaya
Keyword(s):  
Kinetic Model ◽  
Oscillatory Activity ◽  
Adenosine Triphosphatases ◽  
P Type
Sign in / Sign up

Export Citation Format

Share Document