Alkaline Phosphatase and Phosphodiesterase Activities of the Brush Border Membrane of Four Strains of the Tapeworm, Hymenolepis diminuta

1986 ◽  
Vol 72 (5) ◽  
pp. 809 ◽  
Author(s):  
Peter W. Pappas ◽  
David A. Leiby
1972 ◽  
Vol 28 (4) ◽  
pp. 385-386 ◽  
Author(s):  
U. Schmidt ◽  
U. C. Dubach ◽  
I. Bieder ◽  
B. Funk

1985 ◽  
Vol 97 (5) ◽  
pp. 1461-1466 ◽  
Author(s):  
Kazuyuki HIRANO ◽  
Yuichi IIIZUMI ◽  
Yukio MORI ◽  
Kazumi TOYOSHI ◽  
Mamoru SUGIURA ◽  
...  

1984 ◽  
Vol 246 (6) ◽  
pp. F853-F858
Author(s):  
A. K. Mircheff ◽  
H. E. Ives ◽  
V. J. Yee ◽  
D. G. Warnock

A conventional brush border membrane preparation, obtained by divalent cation precipitation of homogenates of rabbit renal cortex, was analyzed by countercurrent distribution in an aqueous dextran:polyethylene glycol two-phase system. The resulting fractions were assayed for the presence of the Na+/H+ antiporter and for a variety of biochemical marker enzymes. This analysis revealed four physically distinct membrane populations (A-D). Population A consisted of two subpopulations, A' and A", which were enriched an average of 49-fold in maltase; they were also highly enriched in alkaline phosphatase, leucine aminopeptidase, and Na+/H+ antiporter. On the basis of their marker contents, populations A' and A" appear to represent highly purified, functional brush border membrane vesicles. Population B was enriched twofold in NADPH-cytochrome c reductase and population C was enriched 12-fold in galactosyltransferase. Populations B and C accounted for 25% of the protein in the starting material and appear to reflect contamination of the brush border membrane preparation by subpopulations of endoplasmic reticulum and Golgi fragments. Population D was enriched in Na+/H+ antiporter, alkaline phosphatase, leucine aminopeptidase, Na-K-ATPase, and acid phosphatase but not maltase, NADPH-cytochrome c reductase, galactosyltransferase, or succinate dehydrogenase. Its identity is unclear, and it might consist of a multiplicity of populations from different origins.


2006 ◽  
Vol 96 (6) ◽  
pp. 1087-1094 ◽  
Author(s):  
Neelam Farooq ◽  
Shubha Priyamvada ◽  
N. A. Arivarasu ◽  
Samina Salim ◽  
Farah Khan ◽  
...  

During Ramadan, Muslims the world over abstain from food and water from dawn to sunset for a month. We hypothesised that this unique model of prolonged intermittent fasting would result in specific intestinal and liver metabolic adaptations and hence alter metabolic activities. The effect of Ramadan-type fasting was studied on enzymes of carbohydrate metabolism and the brush border membrane of intestine and liver from rat used as a model. Rats were fasted (12 h) and then refed (12 h) daily for 30 d, as practised by Muslims during Ramadan. Ramadan-type fasting caused a significant decline in serum glucose, cholesterol and lactate dehydrogenase activity, whereas inorganic phosphate increased but blood urea N was not changed. Fasting resulted in increased activities of intestinal lactate (+34 %), isocitrate (+63 %), succinate (+83 %) and malate (+106 %) dehydrogenases, fructose 1,6-bisphosphatase (+17 %) and glucose-6-phosphatase (+22 %). Liver lactate dehydrogenase, malate dehydrogenase, glucose-6-phosphatase and fructose 1,6-bisphosphatase activities were also enhanced. However, the activities of glucose-6-phosphate dehydrogenase and malic enzyme fell significantly in the intestine but increased in liver. Although the activities of alkaline phosphatase, γ-glutamyl transpeptidase and sucrase decreased in mucosal homogenates and brush border membrane, those of liver alkaline phosphatase, γ-glutamyl transpeptidase and leucine aminopeptidase significantly increased. These changes were due to a respective decrease and increase of the maximal velocities of the enzyme reactions. Ramadan-type fasting caused similar effects whether the rats fasted with a daytime or night-time feeding schedule. The present results show a tremendous adaptation capacity of both liver and intestinal metabolic activities with Ramadan-type fasting in rats used as a model for Ramadan fasting in people.


1981 ◽  
Vol 59 (6) ◽  
pp. 911-917 ◽  
Author(s):  
M. S. Rahman ◽  
D. F. Mettrick ◽  
R. B. Podesta

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.


1980 ◽  
Vol 190 (2) ◽  
pp. 473-476 ◽  
Author(s):  
H S Tenenhouse ◽  
C R Scriver ◽  
E J Vizel

We studied (1) the effect of primary modulators of phosphate transport, namely the hypophosphataemic mouse mutant (Hyp) and low-phosphorus diet, on alkaline phosphatase activity in mouse renal-cortex brush-border membrane vesicles and (2) the effect of several primary inhibitors of alkaline phosphatase on phosphate transport. Brush-border membrane vesicles from Hyp-mouse kidney had 50% loss of Na+-dependent phosphate transport, but only 18% decrease in alkaline phosphatase activity. The low-phosphorus diet effectively stimulated Na+/phosphate co-transport in brush-border membrane vesicles (+ 118%), but increased alkaline phosphatase activity only slightly (+13%). Levamisole (0.1 mM) and EDTA (1.0 mM) inhibited brush-border membrane-vesicle alkaline phosphatase activity of 82% and 93% respectively, but had no significant effect on Na+/phosphate co-transport. We conclude that alkaline phosphatase does not play a direct role in phosphate transport across the brush-border membrane of mouse kidney.


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