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Query: UMLS:C0042961 (volvulus)
 4,305 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A technique employing Sephadex G25 gel filtration has been developed for the rapid isolation and purification of live microfilariae of Onchocerca volvulus from subcutaneous nodules and skin samples. Microfilariae, adult worms and L3 larvae have been surface radiolabelled using the Iodogen technique. Two proteins have been characterised on the surface of uterine microfilariae: these have apparent molecular weights of 14,800 and 15,000. A MW 15,000 protein was the only molecule labelled on the surface of skin microfilariae. Ten proteins were labelled on adult male worms: these have molecular weights of 15,000, 17,500, 20,000, 22,000, 24,000, 29,000, 32,000, 37,000, 42,000, and 50,000. Some, if not all, of these proteins were also identified on female worms. Seven proteins were labelled on the surface of L3 larvae: these have molecular weights of 17,500, 48,000, 50,000, 52,000, 54,000, 57,000, and 105,000. Three of the adult surface proteins were precipitated by selected human infection serum: these are the MW 17,500, 32,000 and 42,000 molecules. The microfilarial surface proteins were not precipitated by human infection serum. The antiserum used in these experiments was shown by Western blot analysis to contain high levels of antibody with specificity for microfilarial and adult antigens. Indirect immunofluorescent assays showed these sera to contain antibody which bound to the surface of adult worms and eggs but not microfilariae. The possibility that skin microfilariae absorb host serum albumin was investigated: Western blot analysis and surface immunofluorescence assays using a specific anti-human albumin serum gave negative results. Fluorescent lectin binding studies revealed the presence of stage-specific carbohydrate moieties exposed on the surface of adult worms and eggs. Microfilariae do not have surface carbohydrate determinants.
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PMID:Surface components of Onchocerca volvulus. 396 55

The objectives of this study were to investigate the determinants of the anion gap (AG) in cattle and to evaluate the utility of AG in detecting hyperlactatemia in sick neonatal calves and adult cattle. The AG was calculated as AG = ([Na+] + [K+])-([Cl-] + [HCO-3]), with all values in mEq/L. The AG of healthy neonatal calves (n = 16) was 29.6 +/- 6.2 mEq/L (mean +/- SD), and the blood L-lactate concentration ranged from 0.5 to 1.2 mM/L. The AG was significantly (P < .05) correlated with serum phosphate (r = .66) and creatinine (r = .51) concentrations. The AG of neonatal calves with experimentally induced diarrhea (n = 16) was 28.6 +/- 5.6 mEq/L, and the blood L-lactate concentration ranged from 1.1 to 2.9 mM/L. The AG was significantly correlated with blood L-lactate concentration (r = .67), serum phosphate concentration (r = .63), creatinine concentration (r = .76), and blood pH (r = -.61). The AG of adult cattle with abomasal volvulus (n = 41) was 20.5 +/- 7.8 mEq/L, and the blood L-lactate concentration ranged from 0.6 to 15.6 mM/L. The AG was significantly correlated with blood L-lactate concentration (r = .60), serum phosphate concentration (r = .71), creatinine concentration (r = .65), albumin concentration (r = .47), total protein concentration (r = .54), blood pyruvate concentration (r = .67), and blood pH (r = -.41) but not plasma beta-OH butyrate concentration. The results indicate that the AG in cattle is only moderately correlated with blood L-lactate concentration and is similarly correlated with serum phosphate and creatinine concentrations in neonatal calves and adult cattle, as well as with serum albumin and total protein concentrations in adult cattle. Anion gap determination is of limited usefulness in predicting blood L-lactate concentration in sick cattle, whereas the correlation between AG and serum creatinine concentration in sick cattle suggests that an increased AG should alert the clinician to the potential presence of uremic anions.
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PMID:Determinants and utility of the anion gap in predicting hyperlactatemia in cattle. 912 93

The mechanism by which filarial parasites derive fatty acids bound to the host's carrier protein is poorly understood. The capacity of a secretory protein of Onchocerca volvulus (OvS1/Ov20) to compete with serum albumin for arachidonic and other fatty acids was investigated in this study. Binding affinities of the two proteins for the long-chain fatty acids were determined using displacement assays. The fluorescent probes used included 11-((5-dimethylaminonaphthalene-1-sulfonyl)amino) undecanoic acid (DAUDA) and cis-parinaric acid. OvS1 protein bound arachidonic acid with an affinity five-fold greater than the affinity exhibited by serum albumin. Oleic acid was bound by the parasite protein with an affinity two-fold greater than the affinity shown by serum albumin. Furthermore, the affinities exhibited by OvS1 protein in binding arachidonic and linoleic acid were about two times higher than the affinity for oleic acid. The results suggest that the OvS1 protein has the capacity to compete with the main host's fatty acid carrier protein for the long-chain fatty acids, in particular arachidonic acid, the precursor for eicosanoids.
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PMID:The secretory Onchocerca volvulus protein OvS1/Ov20 exhibits the capacity to compete with serum albumin for the host's long-chain fatty acids. 1069 49