Studies on plasma membranes III. Mg2+-ATPase, (Na+-K+-Mg2+)-ATPase and 5′-nucleotidase activity of plasma membranes isolated from rat liver

Emmelot, P.; Bos, Cécile

doi:10.1016/0926-6585(66)90304-9

Cited by 244 publications

(41 citation statements)

References 30 publications

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“…Thus it appears that the frequency-dependent increase in contractility might be related to an inhibition of the sarcolemmal Na+-K+-ATPase. (Charnock & Post, 1963;Emmelot & Bos, 1966). However, the present results show that there was no significant change in temperature of the reaction mixture due to electrical stimulation possibly because of the controlled temperature water bath.…”

Section: Discussioncontrasting

confidence: 51%

Frequency‐dependent Changes in the Cardiac Sarcolemmal Atpase

Khatter

Prasad

1977

British J Pharmacology

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1Effects of various frequencies (0.25, 0.5, 1.0, 1.5 or 2.0 Hz) of stimulation for various durations (2, 5, 10 or 15 min) on the contractile force of trabecular or papillary muscles of dog myocardium were investigated. 2Effects of various frequencies (0, 0.25, 0.5, 1.0, 2.0 Hz) of various stimulus strengths (0.5, 1, 10 V) for various durations (2, 5, 10 or 15 min) on the Mg2+‐dependent Na+‐K+‐adenosinetriphosphatase (ATPase) of isolated sarcolemmal fraction of dog myocardium were determined. 3There was a frequency‐dependent increase in the contractility and inhibition of the Na+‐K+‐ATPase within 2 minutes. 4Frequency‐dependent increase in the contractility and inhibition of Na+‐K+‐ATPase decreased as the duration of stimulation was increased. 5The diminution in the inhibition of ATPase was associated with a decrease in the contractility with prolonged stimulation. 6These results suggest that the frequency‐dependent increase in the myocardial contractility might be mediated through an inhibition of the sarcolemmal ATPase.

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Section: Discussioncontrasting

confidence: 51%

Frequency‐dependent Changes in the Cardiac Sarcolemmal Atpase

Khatter

Prasad

1977

British J Pharmacology

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“…Since the enzyme system is localized in membranes, deoxycholate has been successfully used to increase (Na+-K+)-ATPase activity, permitting access of substrate to the enzyme site (65). But, in the liver this detergent inhibits activity (66), and therefore we used the techni(lue of freezethawing samples in hypotonic NaHCO3 to increase activity. Since Vmax increases, indicating an increased number of transport sites, and the apparent Km is unaltered, this method apparently increases activity without altering the structure of the enzyme.…”

Section: Discussionmentioning

confidence: 99%

Stimulation of hepatic sodium and potassium-activated adenosine triphosphatase activity by phenobarbital. Its possible role in regulation of bile flow.

Simon¹,

Sutherland²,

Accatino³

1977

J. Clin. Invest.

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“…These enzymes are markers of plasma membranes, and are highly de pendent on lipids since both of their activities are lost by lipid extraction or phospholipase treatment of membranes (6). This indicates that CC14 disturbs the lipid structure of mem branes, causing a loss of Mg`-ATPase activity.…”

Section: Discussionmentioning

confidence: 99%