Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.4.1 (phosphodiesterase)
 18,767 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rat serum 5'-nucleotidase, L-leucyl-beta-naphthylamidase and beta-glycerophosphatase activities are increased whilst alkaline p-nitrophenylphosphatase and alkaline phosphodiesterase activities are unchanged or decreased three days after bile duct ligation. Affinity chromatography on an immobilised antiserum raised against highly purified liver plasma membranes showed that although 5'-nucleotidase in normal serum is unrelated to the 5'-nucleotidase of liver plasma membrane, the 5'-nucleotidase of bile and much of the 5'-nucleotidase in the jaundiced serum are closely related to the plasma membrane enzyme. Since bile is rich in 5'-nucleotidase, the changes in level of this enzyme after bile duct ligation are most simply explained by leakage of bile into the blood; changes in the patterns of the other enzymes are shown to be consistent with this explanation. The jaundiced serum was examined by gel exclusion chromatography and flotation in sucrose gradients for the presence of small fragments of plasma membrane as reported in human jaundiced sera, but no such fragments could be detected three days after bile-duct ligation.
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PMID:Bile 5'-nucleotidase in the serum of jaundiced rats. 89 Sep 46

1. Incubation of Schistosoma mansoni for 5 min in a phosphate-buffered medium, pH 7.4, released tegumental material containing the following phosphohydrolase activities: alkaline phosphatase, 5'-nucleotidase, glycerol-2-phosphatase, glucose 6-phosphatase, phosphodiesterase and ATPase. 2. Maximum activity of these enzymes was measured at pH 9.5; however, the phosphodiesterase and ATPase activities were also appreciable at pH 7.0. 3. Solubilization of the released tegumental material in 1% Triton X-100 followed by gel filtration distinguished three peaks of enzyme activity: an ATPase (mol.wt. greater than 1000 000), a phosphodiesterase (mol.wt. 1 000 000) and an alkaline phosphomonoesterase with broad specificity (mol.wt. 232 000). 4. The ATPase activity was highly activated by 10 mM-Mg2+ or 1 mM-Ca2+ and was inhibited by chelating agents. Ouabain, Na+ and K+ had little effect on enzyme activity, whereas activity was increased by 50% in the presence of calmodulin. The phosphodiesterase activity was highest in the presence of 100 mM-Na+ or -K+, and 10 mM-Mg2+ or -Ca2+. Alkaline phosphatase activity was also stimulated by 100 mM-Na+ or -K+, and 10 mM-Mg2+; however Ca2+ inhibited at greater than 1 mM. 5. Surface iodination of parasites followed by detergent solubilization and gel filtration of the released tegumental membranes indicated that these enzymes were not accessible. A major surface component, apparent mol.wt. 80 000, was iodinated. 6. Rabbit anti-(mouse liver 5'-nucleotidase) antibodies did not inhibit the phosphohydrolase activities. However, an immunoglobulin G fraction from sera of mice chronically infected with S. mansoni partially inhibited alkaline phosphatase activity, but was without effect on the phosphodiesterase and ATPase activities. 7. The location of the enzymes in the double membrane of the tegument and their significance in host-parasite interactions is discussed.
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PMID:Properties of a series of tegumental membrane-bound phosphohydrolase activities of Schistosoma mansoni. 627 49