Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0042961 (volvulus)
 4,305 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The origin of increased alkaline phosphatase (ALP) activity in peritoneal fluid (PF) of horses with clinical signs of abdominal pain was investigated to determine the usefulness of measuring ALP in PF in the diagnosis of small intestinal injury. The ALP isoenzymes in PF from 10 clinically normal horses and from 50 horses with clinical signs of acute abdominal pain were analyzed for their sensitivities to inhibition by L-phenylalanine, L-homoarginine, and levamisole and to inactivation by heat (56 C, 15 minutes). The enzymes also were discriminated by their patterns of migration during polyacrylamide gel disc electrophoresis. Of 50 horses with colic, 20 had ALP activity in PF at least 3 times the upper limit of normal. Of these 20 horses, 10 had marked increases of ALP activity in PF ranging from 10 to 150 times the mean value of activity as determined in the 10 normal horses. In the 50 horses with colic, ALP values in serum were within the normal range. In 19 of the 20 sick horses, the ALP in PF had properties different from small intestinal ALP. Of the 10 PF samples with markedly increased ALP activity, 9 had a group of properties that were unique for granulocytic ALP. The clinical diagnoses for the 10 horses with markedly increased ALP activity in PF included thromboembolic colic (4 horses), colonic torsion (2 horses), small intestinal volvulus (2 horses), peritonitis (1 horse), and salmonellosis (1 horse). Properties of the enzyme in the 10 PF samples with moderately increased ALP activity were compatible with a granulocytic origin, but insufficient enzyme concentration precluded electrophoretic confirmation of the source. The PF from 1 horse had a mixture of ALP isoenzymes derived from granulocytes and small intestinal mucosa. Of the 50 horses with colic, 6 had severe small intestinal disease without increased ALP activity in PF. Apparently, increased ALP activity in PF cannot be used as a reliable indicator of small intestinal injury in horses, because the ALP is predominantly granulocytic in origin.
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PMID:Origin an importance of increased alkaline phosphatase activity in peritoneal fluids of horses with colic. 725 13

An Onchocerca secretory alkaline phosphatase (E.C. 3.1.3.1) of molecular weight 90 kDa when in crude extract, but which dimerises to about 180 kDa upon purification, was detected, purified and characterised. The enzyme was found to be secreted by both O. ochengi and O. volvulus worms. It was shown to be of Onchocerca origin by Western blotting with bovine onchocerciasis sera and by its time-dependent release in cultures. The O. ochengi enzyme was purified to near homogeneity by a combination of polyethylene glycol precipitation, DEAE-cellulose chromatography and preparative electrophoresis. About 0.96 mg of the active enzyme was purified from 48.4 mg of the crude parasite-released products, giving a purification fold of 71.45 and a yield of 8.7%. The purified enzyme exhibited a typical Michaelis-Menten kinetics with optimum activity on p-nitrophenylphosphate (p-NPP) at pH 10.2. Its apparent K(m) for p-NPP was 0.56+/-0.03 mM and it required Mg(2+) and dithiothreitol (DTT) for stability throughout its purification. Sodium dodecyl sulphate at 2% (w/v) did not inhibit the enzyme activity, but apparently stabilised it during freezing. Inorganic phosphate inhibited the enzyme competitively with an apparent inhibition constant (K(i)) of 3.33+/-0.04 mM, whereas l-phenylalanine inhibited it in a mixed way with a K(i) of 3.18+/-0.03 mM. While contributing to the understanding of metabolism in Onchocerca, the present apparently unique enzyme which is likely to serve in the nutrition of the parasite could be further characterised as a macrofilaricide target or diagnostic marker in onchocerciasis.
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PMID:Detection, purification and characterisation of a secretory alkaline phosphatase from Onchocerca species. 1785 Aug 99