Separation of serum prednisolone and prednisolone-21-hemisuccinate by extraction and their concurrent determination by radioimmunoassay.

1980 ◽  
Vol 26 (9) ◽  
pp. 1301-1303 ◽  
Author(s):  
K Yanagibashi ◽  
A Mizuchi ◽  
H Yotsumoto ◽  
Y Miyachi

Abstract We describe a simple, sensitive, and reliable radioimmunoassay for prednisolone and prednisolone-21-hemisuccinate in serum. The antiserum produced in rabbits to prednisolone-21-hemisuccinate/bovine serum albumin was specific for prednisolone and prednisolone-21-hemisuccinate. A simple dichloromethane extraction permitted the separation of prednisolone from prednisolone-21-hemisuccinate in the serum samples. Interference by cortisol, although not insignificant, is minimized in this assay. We used the method to measure prednisolone and prednisolone-21-hemisuccinate concentrations after a bolus injection of prednisolone-21-hemisuccinate into human beings and mice.

2005 ◽  
Vol 2005 (4) ◽  
pp. 316-321 ◽  
Author(s):  
Medhat Haroun

This report evaluates the significance of antibody/bovine serum albumin (BSA) interactions as a risk factor for the diagnosis of acute hepatitis E. Serum samples from 40 patients with acute hepatitis E and from 40 age/sex matched healthy adult subjects were tested for IgA, IgG, and IgM by ELISA and by turbidimetric assay. BSA was used as a target to characterize changes in levels of interacting immunoglobulins. Initial results obtained before removal of antibodies that interacted with BSA suggested that HEV patients had increased levels of IgM in their sera. It was found that normal individuals had mean IgA, IgG, and IgM levels of2.55mg/mL,9.80mg/mL, and1.73mg/mL, respectively while HEV patients had mean levels of2.66mg/mL,10.04mg/mL, and2.01mg/mL (P<.26,P<.32, andP<.0004). However, the mean level of IgM in HEV-infected sera after purification from antibodies that interacted with BSA was determined to be1.72mg/mL indicating that there was no significant difference in IgM level in HEV patients compared to normal individuals (P<.6). The presence of antibodies that interact with BSA might serve as a diagnostic tool for detection of high-risk patients.


1960 ◽  
Vol 198 (6) ◽  
pp. 1355-1360 ◽  
Author(s):  
Geronimo Terres ◽  
W. L. Hughes ◽  
W. Wolins

Mice were injected with I131-labeled human or bovine serum albumin and determinations made of the rate of loss of radioactivity a) from the whole body ( in vivo counting), b) from the blood (serum samples), and c) from the total trichloroacetic acid precipitable mouse proteins (following homogenization). Measurements by each method made more than 8 hours post-injection gave the same half life (14.5 ± 0.5 hr.) for I131 bovine serum albumin (I131 BSA) when the level of circulating iodide was sufficient to prevent thyroidal accumulation (I131 HSA had a half time of 21 hr.). The variations observed between the methods in the first 24 hours can be explained in terms of times required for the several compartments to reach secular equilibrium, and therefore whole-body measurements in vivo can be safely used to measure the rate of degradation of this protein when allowance for these factors is made.


1989 ◽  
Vol 35 (7) ◽  
pp. 1408-1415 ◽  
Author(s):  
M J Power ◽  
J P Gosling ◽  
P F Fottrell

Abstract We have developed and thoroughly validated radioimmunoassays (RIAs) for osteocalcin in plasma and serum, demonstrating independence of volume and determining the recovery of added standard and within- and between-assay precision. Antibodies were raised in rabbits and mice by immunization with either osteocalcin adsorbed to polyvinylpyrrolidone or osteocalcin conjugated to bovine serum albumin. In both species, use of the conjugated osteocalcin was more efficacious. Correlation of the results obtained when groups of plasma or serum samples were analyzed by RIAs with different antibodies (two polyclonal and one monoclonal) indicated that the normal range observed for osteocalcin concentrations in serum depends on the antibody used. These findings may account for the wide range of "normal" osteocalcin values reported by different groups.


1942 ◽  
Vol 49 (1) ◽  
pp. 96-98 ◽  
Author(s):  
H. A. Davis ◽  
A. G. Eaton ◽  
J. Williamson

2020 ◽  
Vol 27 (08) ◽  
pp. 1747-1752
Author(s):  
Sadaf Shafique ◽  
Raheel Khan ◽  
A.H. Nagi ◽  
Asma Fayyaz ◽  
Afra Samad ◽  
...  

Objectives: To see the detrimental effects of arsenic kushta (kushta-e-Sammulfur) induced toxicity in wistar rats. Study Design: Experimental Study. Setting: Department of Morbid Anatomy and Histopathology, University of Health Sciences, Lahore. Period: 02nd June 2016 to 30th September 2016. Material & Methods: This experimental study was conducted on a total of 48 wistar rats, each weighing approximately, 200-300grams. These rats were then randomly divided into four groups each of them comprising of 12 rats. Group I was taken as a control group which was given flour pellets. Group II was given a single dose of 180 mg/kg of arsenic kushta for 2 weeks, whereas Groups III was given 150 mg/kg of arsenic kushta only for 12 weeks and Group IV was also given dose of 150 mg/kg of arsenic kushta along with 75mg of Bovine Serum Albumin for 12 weeks. Histopathological changes were then seen in the germinal epithelium, stages of spermatogenesis and insterstitium of testes of rats. Results: Changes in germinal epithelium, stages of spermatogenesis and interstitium were seen in all the above groups except group 1 which was the control group. Maximum changes were seen in groups C and D which were given high doses of arsenic kushta along with injection of bovine serum albumin. Conclusion: Arsenic kushta preparation of kushta-e-Summulfur causes testicular toxicity in wistar rats and have similar toxic effects in human beings.


Author(s):  
G. D. Gagne ◽  
M. F. Miller

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.


1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.


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