The alkaline phosphatases present on isolated brush border and basal lateral membranes of rat duodenal epitheilum were examined by means of a variety of biochemical assays and physical methods. The two alkaline phosphatases have similar pH optima of 9.6-9.8, similar substrate km's for p-nitrophenyl
Phosphorylable proteins and alkaline phosphatase of brush border membranes from different parts of the rat small intestine
✍ Scribed by Léa Razanamaniraka; Sylviane Tardivel; Zofia Porembska; Yvonne Dupuis; Gabriel Crouzoulon
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 695 KB
- Volume
- 19
- Category
- Article
- ISSN
- 0020-711X
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The isolated brush border membrane of the tapeworm, Hymenolepis diminuta, hydrolyzes p-nitrophenyl phosphate over a broad pH range. Acid phosphatase activity (pH optimum at 4.0) is inhibited specifically by sodium dodecyl sulfate (SDS) and NaF, while the alkaline phosphatase activity (pH optimum at
## Abstract Incubation of placental brush border membrane (BBM) along with sonicated vesicles of exogenous lipids (egg yolk PC) in the presence of phospholipid‐transfer protein (PL‐TP) showed a decrease in the alkaline phosphatase activity due to the change in the membrane micro‐environment, such a
In the presence of an NaSCN gradient phlorizin binds with a high affinity (Kd 4.7 pM) t o vesicles derived from brush border membranes of intestinal cells of rabbits. The value for Kd corresponds closely t o that of Ki determined from phlorizin inhibition of sugar transport. The apparent affinity fo