Inhibition of human erythrocyte calpain I by novel quinolinecarboxamides
✍ Scribed by Todd L. Graybill; Roland E. Dolle; Irennegbe K. Osifo; Stanley J. Schmidt; Jill S. Gregory; Alex L. Harris; Matthew S. Miller
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 308 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0960-894X
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Methamidophos (O, S‐dimethyl phosphoramidothioate) inhibition of human erythrocyte and plasma cholinesterase was studied __in vitro.__ The pseudo‐biomolecular rate constant of inhibition was 3.14 ± 0.22 × 10^3^ M^−1^ min^−1^ for erythrocyte cholinesterase and 1.85 ± 0.01 × 10^3^ M^−1^ m
## Abstract The inhibition of glucose transport by the non‐ionizable local‐anesthetic benzylalcohol is of the mixed type and independent of pH. The affinity of benzylalcohol to the free carrier is about three times larger than that to the carrier‐glucose complex.
The human erythrocyte membrane carriers for hexoses and nucleosides have several structural features in common. In order to assess functional similarities, the effects of adenosine derivatives on hexose transport and cytochalasin B binding sites were studied. Adenosine inhibited zero-trans uptake of
The effect of increasing single oral doses of the novel catechol-O-methyltransferase (COMT) inhibitor, nitecapone, on enzyme activity in red cells (RBC) and gastroduodenal COMT activity has been studied in healthy male volunteers. A dose-dependent decrease in RBC COMT activity was seen in all cases