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R Wierichs

Publications and source records attributed to R Wierichs.

6 recordsLinked to original sources
PubMed1981

[Mechanism of action of AR-L 115 BS compared to caffeine].

The influence of 2-[(2-methoxy-4-methylsulfinyl)phenyl]-1H-imidazo[4,5-b]pyridine (AR-L 115 BS) and caffeine on Ca++-ATPase activity, Ca++-uptake and Ca++-release (efflux greater than influx:release) of the vesicles of sarcoplasmic reticulum of pig heart was investigated. In contrast to caffeine, 1 mmol/l AR-L 115 BS produced partial inhibition of Ca++-uptake of the vesicle while Ca++-release was only slightly affected. It was not possible to determine the effect of high concentrations of AR-L 115 BS and caffeine on the Ca++-ATPase activity because these substances showed a marked interference with the reagents of the reaction mixture.

Animals↗
PubMed1980

Influence of monovalent ions on the activity of the (Ca2+ + Mg2+)-ATPase and Ca2+ -transport of human red blood cells.

In reconstituted human red blood cells a difference was found in (Ca2+ + Mg2+)-ATPase activity and in Ca2+ efflux at 37 degrees C, depending on the side of the membrane at which the monovalent cations K+ and Na+ were placed. Under the conditions used, (Ca2+ + Mg2+)-ATPase activity and Ca2+ efflux was highest when K+ (35 +/- 0.5 mM (+/- S.E.), mean of four experiments) was at the inside and Na+ (130 mM) at the outside of the ghost membrane.

Biological Transport, Active↗
PubMedDate not supplied

Vanadate inhibition of the Ca++-ATPase of sarcoplasmic reticulum from pig heart.

Ca++-ATPase of sarcoplasmic reticulum from pig heart can be inhibited by vanadate with half maximal inhibition at about 10(-5)M NH4VO3. At the same time vanadate lowers the [Mg++] for maximal activity of the Ca++-ATPase to half, from 8 X 10(-3)M to 4 X 10(-3)M Mg++. At low vanadate concentrations around 5 X 10(-8)M the Ca++-ATPase was activated.

Animals↗