Publications by authors named "Cadman H"

Immunoglobulins were precipitated from pooled African elephant sera with ammonium sulphate and separated by gel filtration and fast protein liquid chromatography (ion exchange). Analysis of the fractions by SDS-PAGE showed IgG of 150 kDa with up to five subclasses, each having heavy chains of 57 kDa and light chains of 27 kDa. Three monoclonal antibodies against human IgG and polyclonal antibodies against canine, bovine, cameline, equine, phocine and feline IgG showed strong cross-reactivity with the African elephant IgG subclasses.

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Reactivity of ostrich sera to Newcastle disease virus (NDV) by enzyme-linked immunosorbent assay (ELISA) and haemagglutination inhibition (HI) test were compared. Ten-month old ostriches seronegative by both tests were vaccinated with an oil-based NDV vaccine on days 0 and 11. Significant levels of reactive antibodies were first detected on day 11 by ELISA (sample/positive ratio > 0.

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A simplified version of the magnetic bead antigen-capture enzyme-linked immunoassay (MBAC-EIA) was used to detect circulating anodic antigen (CAA) in individuals of different age groups with Schistosoma haematobium infection only in an endemic area of Zimbabwe. An overall positive correlation between S. haematobium egg excretion and CAA levels was demonstrated.

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Antibody responses to soluble Schistosoma haematobium egg (SEA) and worm (SWA) antigens in a rural Zimbabwean study population were examined by ELISA. One hundred and sixteen S. haematobium infected and 124 non-infected individuals representing individuals greater than five years old, were included.

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Sera from 216 ostriches on nine farms around Zimbabwe were examined by indirect fluorescent antibody (IFA) testing for the presence of antibodies reactive with Cowdria ruminantium, Coxiella burnetii, and Rickettsia africae, a spotted fever group rickettsia. Although no reactive antibodies could be detected to C. ruminantium or C.

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In the present study, simplification and adaptation of the Magnetic Bead Antigen Capture Enzyme Immuno Assay (MBAC-EIA) technique for detection of circulating anodic antigens (CAA) under field conditions was achieved. It was shown that the assay could be performed successfully within the broad temperature range of 18-37 degrees C. The slightly lower sensitivity observed at low temperatures could be adjusted for by prolonging the incubation period.

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Horseradish peroxidase-conjugated goat anti-ostrich IgG was raised and used in commercial enzyme-linked immunosorbent assay kits to detect antibodies reactive with 11 poultry pathogens in sera from 149 ostriches from nine farms around Zimbabwe. Antibodies were detected to turkey rhinotracheitis virus (99%), Newcastle disease virus (23%), avian reovirus (19%), infectious bursal disease virus (15%), avian encephalomyelitis virus (15%), Mycoplasma gallisepticum and/or M. synoviae (11%), reticuloendotheliosis virus (10%), Salmonella enteritidis (8%), avian leukosis virus (3%), infectious bronchitis virus (2%), and Pasteurella multocida (< 1%).

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Immunoglobulins were separated from ostrich sera by ammonium sulfate precipitation and ion-exchange chromatography. Two classes of immunoglobulin could be identified, corresponding to IgG and IgM of other species, based on elution profiles from ion-exchange columns and molecular mass estimation on gel-filtration chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). On SDS-PAGE, the heavy chains of IgG and IgM were shown to have molecular masses of 67.

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The binding of 125I-labelled human growth hormone (hGH) to a purified plasma membrane preparation from the liver of pregnant rabbit, and to receptors solubilized from this fraction with Triton X-100, was dependent on time, temperature, the cations used and the receptor concentration. Solubilization did not affect the binding properties of the receptors at low concentrations of Triton X-100. Some somatogenic hormones, such as bovine GH, and some lactogenic hormones, such as ovine prolactin, displaced 125I-labelled hGH from purified plasma membranes and solubilized receptor preparations, but GHs and prolactins from various other species were rather ineffective.

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The characteristics of the binding of homologous and heterologous (human) LDL to membrane preparations from porcine adrenal cortex have been determined. The membranes displayed a single class of high-affinity, saturable binding site for both 125I-labelled porcine and human LDL, which was dependent on divalent cations, in addition to a low-affinity, non-saturable component(s). Porcine LDL displaced both 125I-labelled porcine and 125I-labelled human LDLs from the high-affinity binding site more effectively than human LDL, reflecting the lower Kd, (13.

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The binding of 125I-labelled human somatotropin (growth hormone) to a crude membrane preparation from the liver of pregnant rabbit, and to receptors solubilized from this fraction by Triton X-100, was dependent on time, temperature and receptor concentration. At 4 degrees C a steady state was reached after 20 h, and maximum specific binding (as a percentage of total tracer added) was approx. 50% for both membrane-bound and solubilized receptors.

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