+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Activation and inhibition of the brush-border membrane-bound alkaline phosphatase activity of Hymenolepis diminuta (Cestoda) by divalent cations



Activation and inhibition of the brush-border membrane-bound alkaline phosphatase activity of Hymenolepis diminuta (Cestoda) by divalent cations



Parasitology 102 Pt 1: 141-145



In the absence of exogenous divalent cations, the isolated brush-border plasma membrane of Hymenolepsis diminuta possesses alkaline phosphatase activity (APA). APA is stimulated in the presence of exogenous Mg2+ and inhibited by low concentrations of Zn2+ or high concentrations of Ca2+, and inhibition of APA by Zn2+ is reversed by both Mg2+ and Ca2+. APA is inhibited by ethylenediamine tetraacetic acid (EDTA), ethyleneglycol-bis-(beta-aminoethyl ether) N,N'-tetraacetic acid, and 1,10-phenanthroline in time- and concentration-dependent fashions, with EDTA being the most effective inhibitor. Following treatment with EDTA, APA is restored by Mg2+ and, to a lesser extent, by Ca2+, but not by Zn2+. Thus, APA represents a Mg2(+)-dependent enzyme that can be partly activated by Ca2+ but only in the absence of Mg2+.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 039165044

Download citation: RISBibTeXText

PMID: 1903877

DOI: 10.1017/s0031182000060455


Related references

Solubilization of membrane-bound ribonuclease (RNAse) and alkaline phosphatase from the isolated brush border of Hymenolepis diminuta (Cestoda). Journal of Parasitology 66(3): 434-438, 1980

Ca2+ inhibition of brush border alkaline phosphatase activity in Hymenolepis diminuta. Zeitschrift für Parasitenkunde 71(6): 759-763, 1985

Calcium inhibition of brush border alkaline phosphatase activity in hymenolepis diminuta. Zeitschrift fuer Parasitenkunde 71(6): 759-764, 1985

Acid phosphatase activity in the isolated brush border membrane of the tapeworm, Hymenolepis diminuta: partial characterization and differentiation from the alkaline phosphatase activity. Journal of Cellular Biochemistry 37(4): 395-403, 1988

Hymenolepis diminuta: further characterization of the membrane-bound acid phosphatase activity associated with the brush border membrane of the tapeworm's tegument. Experimental Parasitology 724: 362-367, 1991

Competitive, uncompetitive, and mixed inhibitors of the alkaline phosphatase activity associated with the isolated brush border membrane of the tapeworm Hymenolepis diminuta. Journal of Cellular Biochemistry 40(2): 239-248, 1989

Characterization of membrane-bound enzymes from the isolated brush border plasma membrane of the tapeworm Hymenolepis diminuta (Cestoda). Dissertation Abstracts International B Sciences and Engineering, 417: 2445, 1981

Solubilization of the membrane-bound enzymes of the brush-border plasma membrane of Hymenolepis diminuta (Cestoda) using nonionic detergents. Journal of Parasitology 68(4): 588-592, 1982

Kinetic analyses of the membrane-bound alkaline phosphatase activity of hymenolepis diminuta (Cestoda: Cyclophyllidea) in relation to development of the tapeworm in the definitive host. Journal of Cellular Biochemistry 25(3): 131-137, 1984

Alkaline phosphatase and phosphodiesterase activities of the brush border membrane of four strains of the tapeworm, Hymenolepis diminuta. Journal of Parasitology 72(5): 809-811, 1986

Hymenolepis diminuta: partial characterization of the membrane-bound and solubilized alkaline phosphohydrolase activities of the isolated brush border plasma membrane. Experimental Parasitology 541: 80-86, 1982

Hymenolepis diminuta partial characterization of the membrane bound and solubilized alkaline phospho hydrolase ec 3.1.3.1 activities of the isolated brush border plasma membrane. Experimental Parasitology 54(1): 80-86, 1982

Phosphohydrolase activity of the isolated, brush-border membrane of Hymenolepis diminuta (Cestoda) following sodium dodecyl sulfate (SDS) - polyacrylamide gel electrophoresis. Journal of Parasitology 666: 914-919, 1980

Phosphohydrolase Activity of the Isolated, Brush-Border Membrane of Hymenolepis diminuta (Cestoda) Following Sodium Dodecyl Sulfate (Sds)-Polyacrylamide Gel Electrophoresis. The Journal of Parasitology 66(6): 914-919, 1980

Phospho hydrolase activity of the isolated brush border membrane of hymenolepis diminuta cestoda following sodium dodecyl sulfate poly acrylamide gel electrophoresis. Journal of Parasitology 66(6): 914-919, 1980