Noninvasive analysis of fecal reproductive hormone metabolites in female veiled chameleons (Chamaeleo calyptratus) by enzyme immunoassay

Zoo Biology ◽  
2010 ◽  
pp. n/a-n/a ◽  
Author(s):  
Maya S. Kummrow ◽  
Christine Gilman ◽  
Paula Mackie ◽  
Dale A. Smith ◽  
Gabriela F. Mastromonaco
2013 ◽  
Vol 82 (1) ◽  
pp. 91-96
Author(s):  
Ignacio Ayala ◽  
Nieves Martos

The aim of this work was to measure serum concentrations of dehydroepiandrosterone, androstenedione, testosterone and 17β-oestradiol in horses with various diseases and after surgery. We hypothesize that diseases and castration could potentially affect concentrations of steroid reproductive hormones. Blood samples were obtained from six groups of horses comprising a total of 119 horses (75 males and 44 females, 5–15 years old) with laminitis, acute abdominal syndrome, acute diseases, chronic diseases, after castration and healthy control. Hormone concentrations in serum were determined for each group using competitive enzyme immunoassay. Significant increases compared to control were found for dehydroepiandrosterone in horses with castration (P < 0.01), acute abdominal syndrome and acute diseases (P < 0.05). Besides, significant increases were observed for androstenedione in horses with laminitis, castration and acute diseases (P < 0.01), and in acute abdominal syndrome and chronic diseases (P < 0.05). Significant increases were also found for testosterone in horses with castration (P < 0.01) and with laminitis, acute abdominal syndrome and chronic diseases (P < 0.05). The lowest values of testosterone were found in the control group. Compared to control, 17b-oestradiol serum concentrations showed significant decreases (P < 0.01) in horses with laminitis, acute abdominal syndrome, acute and chronic diseases. Significant differences (P < 0.05) for the four studied hormones were found between males and females in each group. Our results showed that there were significant differences in steroid reproductive hormone concentrations in diseased horses and in those after surgery, compared to controls.


2001 ◽  
Vol 120 (5) ◽  
pp. A492-A493 ◽  
Author(s):  
E HAINDL ◽  
H BENESCH ◽  
A FINCK ◽  
V MUEHISTEIN ◽  
A LEODOLTER ◽  
...  

2001 ◽  
Vol 120 (5) ◽  
pp. A492-A492
Author(s):  
Y YEE ◽  
E YIP ◽  
T QUE ◽  
K LI ◽  
C LEE ◽  
...  

1988 ◽  
Vol 59 (02) ◽  
pp. 310-315 ◽  
Author(s):  
P W Koppert ◽  
E Hoegee-de Nobel ◽  
W Nieuwenhuizen

SummaryWe have developed a sandwich-type enzyme immunoassay (EIA) for the quantitation of fibrin degradation products (FbDP) in plasma with a time-to-result of only 45 minutes.* The assay is based on the combination of the specificities of two monoclonal antibodies (FDP-14 and DD-13), developed in our institute. FDP-14, the capture antibody, binds both fibrinogen degradation products (FbgDP) and FbDP, but does not react with the parent fibrin(ogen) molecules. It has its epitope in the E-domain of the fibrinogen molecule on the Bβ-chain between amino acids 54-118. Antibody DD-13 was raised using D-dimer as antigen and is used as a tagging antibody, conjugated with horse-radish peroxidase. A strong positive reaction is obtained with a whole blood clot lysate (lysis induced by tissue-type plasminogen activator) which is used as a standard. The EIA does virtually not detect FbgDP i. e. purified fragments X, Y, or FbgDP generated in vitro in plasma by streptokinase treatment. This indicates that the assay is specific for fibrin degradation products.We have successfully applied this assay to the plasma of patients with a variety of diseased states. In combination with the assay previously developed by us for FbgDP and for the total amount of FbgDP + FbDP (TDP) in plasma, we are now able to study the composition of TDP in patients plasma in terms of FbgDP and FbDP.


1992 ◽  
Vol 67 (05) ◽  
pp. 507-509 ◽  
Author(s):  
John Gibson ◽  
Margaret Nelson ◽  
Ross Brown ◽  
Hatem Salem ◽  
Harry Kronenberg

SummaryIn order to investigate the possibility that autoantibodies to thrombomodulin (TM) may exist in patients with the lupus anticoagulant (LA) and perhaps be implicated in the pathogenesis of recurrent thrombosis seen in such patients, we developed an enzyme-immunoassay to screen serum samples for anti-human TM activity. The major technical problem encountered in developing this assay was to reduce the non-specific binding of serum components from both the LA positive and the negative population. Considerable reduction of non-specific binding was achieved by use of a phosphate/citrate buffer at pH 8.0 and the use of an optimal sample dilution of 1/40. In addition, samples were always tested in parallel in blank wells and results are expressed as an OD ratio. Samples from 113 patients with the LA were assayed and compared to 78 patients referred for LA testing but found to be negative. The mean OD values for the LA positive patients (± SD) was 1.36 (0.44) with a range of 0.78-2.57. This was virtually identical to the values for the LA negative population (1.38 ± 0.40, range 0.76-2.77). The results of this study indicate that there is no evidence for the presence of a significant autoantibody activity to TM in patients with the LA when compared to LA negative patients. If such autoantibodies do exist their frequency must be quite low.


1985 ◽  
Vol 54 (03) ◽  
pp. 599-602 ◽  
Author(s):  
M Léon Alhenc-Gelas ◽  
M Aiach ◽  
A Gorenflot ◽  
J P Andreux

SummaryImmunoreactive AT III was found in human platelets. AT III antigen was quantified in platelets taken from each of 17 healthy donors by a specific competitive enzyme immunoassay using purified AT III and AT III antibodies. AT III antigen levels in extracts of washed platelets disrupted by freezing and thawing ranged from 32 to 140 ng per 109 platelets with a mean value of 70.3 ± 27.3. When stimulated by arachidonic acid, the platelets released AT III antigen together with immunoreactive fibrinogen. These results show that AT III is present in platelets at a level corresponding to approximately 0.01% of total antithrombin in normal blood, and suggest that platelet AT III, like fibrinogen, is contained in the storage granules.


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