Glycosyl Transferase Activity in the Brush Border Membrane of Hymenolepis diminuta

1983 ◽  
Vol 69 (6) ◽  
pp. 1055 ◽  
Author(s):  
Peter W. Pappas
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Hymenolepis Diminuta ◽  
Transferase Activity ◽  
Glycosyl Transferase

Use of saponin in the preparation of brush border from a parasitic flatworm

1981 ◽  
Vol 59 (6) ◽  
pp. 911-917 ◽  
Author(s):  
M. S. Rahman ◽  
D. F. Mettrick ◽  
R. B. Podesta
Keyword(s):  
Electron Microscopy ◽  
Plasma Membrane ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Hymenolepis Diminuta ◽  
Parasitic Flatworm ◽  
Basal Plasma Membrane ◽  
Basal Plasma

Saponin treatment in hypotonic or hypertonic fluids, followed by vibration, was used to isolate the brush border membrane from the surface epithelial syncytium of Hymenolepis diminuta. Electron microscopy of the membrane pellets and the parasites indicated that the area of the syncytium sheered by vibration of the parasites was correlated with the areas of the syncytium in which there occurred the greatest amount of osmotically induced swelling: below and adjacent to the brush border in hypotonic incubation, and the infoldings of the basal plasma membrane of the syncytium in hypertonic incubations. Vesiculation of the microvilli occurred in incubations made hypertonic with mannitol.

Properties of a Mg2+-dependent, and Ca2+-inhibited ATPase localized in the brush border of the surface epithelial syncytium of a parasitic flatworm

1981 ◽  
Vol 59 (6) ◽  
pp. 918-923 ◽  
Author(s):  
M. Saidur Rahman ◽  
D. F. Mettrick ◽  
R. B. Podesta
Keyword(s):  
Atpase Activity ◽  
Osmotic Pressure ◽  
Brush Border ◽  
Volume Regulation ◽  
Brush Border Membrane ◽  
Ethacrynic Acid ◽  
Surface Membrane ◽  
Hymenolepis Diminuta ◽  
Parasitic Flatworm ◽  
Acid Reaction

The brush border membrane of the surface epithelial syncytium of the parasitic flatworm, Hymenolepis diminuta, was isolated by saponin treatment, and the ATPase activity was determined. The ATPase activity was insensitive to ouabain, SCN−, HCO3−, ethanol, and, although slightly inhibited by high oligomycin concentrations, was inhibited by ethacrynic acid. Reaction mixtures made increasingly hypertonic with mannitol resulted in vesicular changes in the microvilli and decreased ATPase activity. Although treatment of the brush border fraction with deoxycholate increased ATPase activity, the dependence of activity on the osmotic pressure of the reaction mixture persisted in the solubilized membrane preparations. ATPase activity was dependent upon Mg2+ and Na+ + K+ concentration. It is suggested that the ATPase in the flatworm surface membrane is involved in volume regulation in hypotonic media.

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