+ 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

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



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



The membrane-bound and solubilized (using Triton X-100 or sodium dodecyl sulfate [SDS]) alkaline phosphohydrolase (APase) activities of the isolated brush border membrane of H. diminuta [rat parasite] require a divalent cation for maximum activity. Highest rates of substrate (p-nitrophenyl phosphate) hydrolysis are obtained with low concentrations of Mg2+ (1 mM), although low concentration of Mn2+, Ca2+ for Zn2+ will also partially satisfy this requirement; higher concentrations of Mg2+ and Mn2+, and other divalent cations (Cu2+, Fe2+, and Pb2+), inhibit the membrane-bound APase activity. Solubilization of the membrane-bound enzyme in either Triton or SDS results in an increase in specific activity and Km, but has little effect on thermal stability of the APase activity. Phosphate, pyrophosphate, ATP, AMP, glucose 1-phosphate, G-6-P, fructose 6-phosphate and fructose 1,6-diphosphate inhibit substrate hydrolysis, and the relative affinities of these inhibitors for the APase enzyme are altered only slightly upon solubilization. Graphic analyses of data from inhibitor studies indicate that all 8 inhibitors will inhibit membrane-bound and solubilized APase activities 100% at high inhibitor:substrate ratios. Molybdate, F-, 2-mercaptoethanol, cysteine and p-chloromercuribenzoate inhibit membrane-bound APase activity. Inhibitor data indiate that if more than 1 enzyme is responsible for the APase activity of the brush border membrane of H. diminuta, the enzymes cannot be differentiated on the basis of substrate specificity.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 005601573

Download citation: RISBibTeXText


Related references

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 membrane-bound nucleotidase-activities (ATPase and 5'-nucleotidase) in the isolated brush border membrane. Experimental Parasitology 51(2): 209-219, 1981

Nucleotide hydrolysis by solubilized membrane-bound enzymes of the brush border plasma membrane of Hymenolepis diminuta. Molecular and biochemical parasitology 8(1): 1-16, 1983

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

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

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

A comparison of membrane-bound enzymes of the isolated brush border plasma membranes of the cestodes Hymenolepis diminuta and H. microstoma. Parasitology 84(2): 391-396, 1982

Isolation and partial biochemical characterization of the brush border plasma membrane from the cestode, Hymenolepis diminuta. Journal of Parasitology 65(5): 715-731, 1979

Isolation and partial biochemical characterization of the brush border plasma membrane from the cestode Hymenolepis diminuta. Dissertation Abstracts International B Sciences and Engineering, 425: 1718, 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

Partial characterization of ribonuclease (RNase) activity from the isolated and solubilized brush border of Hymenolepis diminuta. Journal of Parasitology 67(3): 372-377, 1981

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

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

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, 1991