The Experts below are selected from a list of 183 Experts worldwide ranked by ideXlab platform
Porntip Prommuang - One of the best experts on this subject based on the ideXlab platform.
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isolation of avian influenza virus a subtype h5n1 from internal contents albumen and Allantoic Fluid of japanese quail coturnix coturnix japonica eggs and oviduct during a natural outbreak
Annals of the New York Academy of Sciences, 2006Co-Authors: Naruepol Promkuntod, Chongmas Antarasena, Porntip PrommuangAbstract:Avian influenza virus (AIV) was recovered from the internal contents of eggs, including mixture of albumen and Allantoic Fluid, and from the oviduct of naturally infected Japanese quail (Coturnix coturnix japonica) flocks in the southern part of Thailand. The virus titers of 10(4.6)-10(6.2) ELD(50)/mL were directly measured from the internal content of infected eggs. The virus was isolated by chorioAllantoic sac inoculation of embryonating chicken eggs. Infected Allantoic Fluid was identified as hemagglutinating virus and then was indicated the presence of H5 hemagglutinin. The virus was confirmed to be H5N1 subtype influenza A virus by reverse transcriptase-polymerase chain reaction. Additionally, real-time reverse transcriptase-polymerase chain reaction assay could specifically detect influenza virus subtype H5. Furthermore, indirect fluorescent antibody (IFA) test by using specific anti-influenza A monoclonal antibody indicated that virus antigens were detected in the parenchyma of multiple tissues. Systemic localization of viral antigen detected was certainly considered to be viremic stage. In addition, influenza virus antigen was also detected by IFA in Allantoic Fluid sediments isolated from internal content of egg or oviduct. The conclusion of isolated AIV type A subtype H5N1 from these two infected materials was correlated to the viremic stage of infection because the virus antigens could be observed in almost all tissues. Conclusively, the need for adequate safeguards to prevent contamination and spread of the virus to the environment during movement of eggs--including hatching eggs, cracked eggs, and other relevant infected materials-- or egg consumption from area of outbreak is emphasized and must not be ignored for the reasons of animal, public, and environmental health.
S Ghadi - One of the best experts on this subject based on the ideXlab platform.
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identification of different serotypes of infectious bronchitis viruses in Allantoic Fluid samples with single and multiplex rt pcr
Iranian Journal of Virology, 2009Co-Authors: M M Rafiei, M Vasfimarandi, M H Bozorgmehrifard, S GhadiAbstract:Background and Aims: Infectious bronchitis virus (IBV) causes an acute, highly contagious respiratory and kidney disease of chickens which results in significant economic losses in commercial broilers, layers and breeders. Rapid identification of IBV serotypes involved in respiratory complex is a problem in the differential diagnosis. Materials and Methods: In this study, a single and multiplex RT-PCR was used to detect group III, Massachusetts and 793/B serotypes of IBV that have been circulating in Iranian poultry industry since 1999. Results: Only seven out of 49 Allantoic Fluid samples showed positive results in single RTPCR using group specific primers. Two of these samples belonged to IBV positive group in VN test. Whereas; four samples belonged to H9N2 positive group and one sample belonged to IBV/AIV negative groups. The high sensitivity of single RT-PCR led to detect some of the missed IBV infections as compared with other virological tests. Three out of 7, IBV isolates identified with single RT-PCR, classified as 793/B serotype and four of them categorized as Massachusetts serotype in multiplex RT-PCR. Conclusion: The results indicated that multiplex RT-PCR method, can be a valuable test for rapid identification of Massachusetts and 793/B serotypes in complex respiratory complex infection of chickens
August Epple - One of the best experts on this subject based on the ideXlab platform.
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hormonal effects on amino acids and related compounds in plasma amniotic Fluid and Allantoic Fluid of the chicken embryo
General and Comparative Endocrinology, 1999Co-Authors: A Hohlweg, Louis Milakofsky, Theodore A. Hare, Barbara Nibbio, Q Tran, August EppleAbstract:So far, more than 40 free amino acids and related compounds have been identified in plasma, amniotic Fluid, and/or Allantoic Fluid of the 13-day chicken embryo. Concentration differences, and greatly varying behavior of these compounds under experimental conditions, revealed the presence of specific barriers among the three Fluids. We tested the hypotheses that (1) the absence of an innervation of amnion and allantois indicates a hormonal control of their barriers, and (2) changes in the concentrations of certain amino compounds in the three Fluids indicate anabolic or catabolic actions of hormones. Insulin, prolactin, and stress caused complex changes of the concentrations of amino compounds in all three Fluids within 30 min. Some of these changes indicated breakdown of embryonic tissues, while others must have been due to transfer of amino compounds among the three Fluid compartments. However, there was no significant effect on the glucose concentration in any of the three compartments under any of the experimental conditions. This is the first demonstration of hormonal effects on the amino compounds in the extraembryonic Fluids of nonmammalian amniotes.
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IMPACT OF ETHANOL STRESS ON COMPONENTS OF THE Allantoic Fluid OF THE CHICKEN EMBRYO
Comparative biochemistry and physiology. Part A Physiology, 1997Co-Authors: M.ten Busch, Louis Milakofsky, Theodore A. Hare, Barbara Nibbio, August EppleAbstract:Recent studies showed that the Allantoic Fluid of the chicken embryo is a depot for stress-released catecholamines and many free amino acids and related compounds, and that it is separated from plasma and the amniotic Fluid by selective barriers. To gain further insights into the functions of the allantois and its barriers, we studied the impact of stress (intra-Allantoic injection of 0.1 ml ethanol) on 39 free amino acids and related compounds of the Allantoic Fluid. Using an HPLC-fluorometric method, we found that the concentration of seven substances was significantly increased 20 min after injection of ethanol, and back to control levels within 40 minutes. Five of these compounds (asparagine, alanine, leucine, tyrosine, lysine) had previously been shown to occur in plasma at concentrations above those in the Allantoic Fluid. However, taurine and phosphoethanolamine increased in the Allantoic Fluid even though their concentrations in plasma tended to be lower than in Allantoic Fluid. These findings (1) reveal the existence of complex embryonic/extraembryonic autoregulations, and (2) raise the question of the regulatory mechanisms involved in the transfer of substances across the Allantoic barrier(s).
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Sulfate conjugates of catecholamines in the Allantoic Fluid of the chicken embryo.
General and comparative endocrinology, 1994Co-Authors: Tejendra S. Gill, Barbara Nibbio, Sepp Porta, August EppleAbstract:In addition to free dopamine (DA), norepinephrine (NE), and epinephrine (E), the Allantoic Fluid of the 13-day-old chicken embryo contains sulfate conjugates of these three catecholamines (CAs). The concentration of DA sulfate is relatively low, while NE and E sulfates occur at levels similar to those of the free fractions. The comparatively low concentration of free CAs in the amniotic Fluid, seen in a previous study, is confirmed. However, the amniotic barrier for sulfated CAs is much stronger, possibly absolute. Though some technical difficulties remain to be resolved, the chicken embryo may become a useful model for the study of the prenatal functions of CA conjugates.
James R. Mcfarlane - One of the best experts on this subject based on the ideXlab platform.
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Uterine Milk Protein, a Novel Activin-Binding Protein, Is Present in Ovine Allantoic Fluid*
Endocrinology, 1999Co-Authors: James R. Mcfarlane, Lynda M. Foulds, Graham Jenkin, Anne E O'connor, David James Phillips, Milton T.w. Hearn, D. M. De KretserAbstract:Activins are pluripotent growth factors that have recently been shown to be present in placental and fetal membrane preparations. Our previous studies have identified and purified activin A from ovine amniotic and Allantoic Fluids. In this study, ligand blots of side fractions from the isolation of activin A from Allantoic Fluid suggested the presence of activin-binding proteins other than follistatin. Further purification of one of these fractions involved two sequential reverse phase HPLC steps and a Superose 12HR fractionation. SDS-PAGE revealed a single protein band of 55 kDa, which was identified by NH2-terminal sequencing as ovine uterine milk protein (UTMP), a member of the serine protease inhibitor (serpin) superfamily of proteins. Further binding studies, using ligand blot techniques and Superose 12HR fractionation in the presence of [ 125 I]activin, demonstrated UTMP to be an activin-binding protein with a lower affinity for activin than that of follistatin. A study of the specific binding behavior of UTMP to activin, using surface plasmon resonance, revealed an apparent equilibrium dissociation constant (Kd )o f 496 25 nM, compared with the follistatin-activin Kd of 379 6 51 pM. Similar to another activin-binding protein, a2-macroglobulin, UTMP was unable to neutralize the bioactivity of activin in a bioassay based on the capacity of activin to inhibit the proliferation of an MPC-11 plasmacytoma cell line. The high concentrations of this protein in uterine Fluid during pregnancy and its ability to bind activin suggest that UTMP may act as a low affinity, high capacity binding protein to sequester activin in the local uterine environment. (Endocrinology 140: 4745‐ 4752, 1999)
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Ovine Allantoic Fluid contains high concentrations of activin A: Partial dissociation of immunoactivity and bioactivity
Biology of reproduction, 1998Co-Authors: Lynda M. Foulds, D. M. De Kretser, Paul G Farnworth, Danielle Buttress, Graham Jenkin, Nigel P. Groome, James R. McfarlaneAbstract:In a preliminary study, Allantoic Fluid collected from pregnant sheep across gestational ages of 20-124 days contained significantly higher levels of activin bioactivity (189 +/- 74 ng/ml, mean +/- SE) than did amniotic Fluid (3.2 +/- 0.6 ng/ml). Using a combination of chromatography steps, we isolated from 5 L of Allantoic Fluid approximately 612 microg of immunoactive activin, which eluted over 10 fractions from a C8 reversed-phase column. When these fractions were assayed in a rat pituitary cell culture bioassay, in a specific RIA, and in an activin A two-site ELISA, the RIA activity was skewed to the less hydrophobic side of the activin profile, while the bioactivity was skewed to the more hydrophobic forms. The activity measured in the two-site ELISA more closely matched the mass of activin as determined by laser densitometry. Amino-terminal sequencing of fractions containing either peak immunoactivity or bioactivity showed each to be identical to activin A. This was confirmed by internal sequences from a fraction that eluted in the area of overlapping immunoactivity and bioactivity. A peptide containing at least 18 amino acids at its amino terminus, which were identical to the conserved region of the acute-phase protein serum amyloid A, was identified in the most immunoactive activin fractions.
D. M. De Kretser - One of the best experts on this subject based on the ideXlab platform.
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Uterine Milk Protein, a Novel Activin-Binding Protein, Is Present in Ovine Allantoic Fluid*
Endocrinology, 1999Co-Authors: James R. Mcfarlane, Lynda M. Foulds, Graham Jenkin, Anne E O'connor, David James Phillips, Milton T.w. Hearn, D. M. De KretserAbstract:Activins are pluripotent growth factors that have recently been shown to be present in placental and fetal membrane preparations. Our previous studies have identified and purified activin A from ovine amniotic and Allantoic Fluids. In this study, ligand blots of side fractions from the isolation of activin A from Allantoic Fluid suggested the presence of activin-binding proteins other than follistatin. Further purification of one of these fractions involved two sequential reverse phase HPLC steps and a Superose 12HR fractionation. SDS-PAGE revealed a single protein band of 55 kDa, which was identified by NH2-terminal sequencing as ovine uterine milk protein (UTMP), a member of the serine protease inhibitor (serpin) superfamily of proteins. Further binding studies, using ligand blot techniques and Superose 12HR fractionation in the presence of [ 125 I]activin, demonstrated UTMP to be an activin-binding protein with a lower affinity for activin than that of follistatin. A study of the specific binding behavior of UTMP to activin, using surface plasmon resonance, revealed an apparent equilibrium dissociation constant (Kd )o f 496 25 nM, compared with the follistatin-activin Kd of 379 6 51 pM. Similar to another activin-binding protein, a2-macroglobulin, UTMP was unable to neutralize the bioactivity of activin in a bioassay based on the capacity of activin to inhibit the proliferation of an MPC-11 plasmacytoma cell line. The high concentrations of this protein in uterine Fluid during pregnancy and its ability to bind activin suggest that UTMP may act as a low affinity, high capacity binding protein to sequester activin in the local uterine environment. (Endocrinology 140: 4745‐ 4752, 1999)
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Ovine Allantoic Fluid contains high concentrations of activin A: Partial dissociation of immunoactivity and bioactivity
Biology of reproduction, 1998Co-Authors: Lynda M. Foulds, D. M. De Kretser, Paul G Farnworth, Danielle Buttress, Graham Jenkin, Nigel P. Groome, James R. McfarlaneAbstract:In a preliminary study, Allantoic Fluid collected from pregnant sheep across gestational ages of 20-124 days contained significantly higher levels of activin bioactivity (189 +/- 74 ng/ml, mean +/- SE) than did amniotic Fluid (3.2 +/- 0.6 ng/ml). Using a combination of chromatography steps, we isolated from 5 L of Allantoic Fluid approximately 612 microg of immunoactive activin, which eluted over 10 fractions from a C8 reversed-phase column. When these fractions were assayed in a rat pituitary cell culture bioassay, in a specific RIA, and in an activin A two-site ELISA, the RIA activity was skewed to the less hydrophobic side of the activin profile, while the bioactivity was skewed to the more hydrophobic forms. The activity measured in the two-site ELISA more closely matched the mass of activin as determined by laser densitometry. Amino-terminal sequencing of fractions containing either peak immunoactivity or bioactivity showed each to be identical to activin A. This was confirmed by internal sequences from a fraction that eluted in the area of overlapping immunoactivity and bioactivity. A peptide containing at least 18 amino acids at its amino terminus, which were identical to the conserved region of the acute-phase protein serum amyloid A, was identified in the most immunoactive activin fractions.
