scholarly journals Radioimmunoassay of colchicine

1975 ◽  
Vol 151 (2) ◽  
pp. 413-415 ◽  
Author(s):  
C Boudene ◽  
F Duprey ◽  
C Bohuon
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Biological Fluids ◽  
Cross Reaction ◽  
Colchicine Derivatives

Antibodies to cholchicine were raised in rabbits after injection of N-desacetylthiocolchicine conjugated to bovine serum albumin. Antisera diluted 1:100 bound 50% of 1.6ng of [3H]colchicine. Cross-reaction of the antisera with colchicine derivatives and other drugs was measured and a radioimmunoassay of colchicine in biological fluids was proposed.

scholarly journals Production and properties of antisera to dexamethasone–protein conjugates

1973 ◽  
Vol 133 (2) ◽  
pp. 401-404 ◽  
Author(s):  
M. C. Dumasia ◽  
D. I. Chapman ◽  
M. S. Moss ◽  
C. O'Connor
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Cross Reaction ◽  
Protein Conjugates ◽  
The Cross

Antibodies to dexamethasone 21-hemisuccinate conjugated to bovine serum albumin were produced in rabbits. Antisera diluted 1:3000 bound 50% of 90pg of [1,2-3H]dexamethasone. The cross-reaction of the antisera with other synthetic and natural corticosteroids was measured.

DEVELOPMENT OF A RADIOIMMUNOASSAY FOR 5α-ANDROST-16-EN-3-ONE IN PIG PERIPHERAL PLASMA

1974 ◽  
Vol 76 (2) ◽  
pp. 377-387 ◽  
Author(s):  
Ø. Andresen
Keyword(s):  
Regression Analysis ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Cross Reaction ◽  
Plasma Samples ◽  
Standard Curve ◽  
Peripheral Plasma ◽  
Accuracy Study ◽  
The Mean

ABSTRACT A radioimmunoassay (RIA) for 5α-androst-16-en-3-one (5α-androstenone) in peripheral plasma from pigs has been developed. Antibodies against 5α-androstenone conjugated through C-3 to bovine serum albumin (BSA) were produced in rabbits. The antiplasma used in this study show a cross-reaction of 100% with 4,16-androstadien-3-one (androstadienone), 5.3 % with 5α-androst-16-en-3β-ol (an-β), 3.3 % with 5α-androst-16-en-3α-ol (an-α), 2.6 % with 4-androstene-3,17-dione (androstenedione) and 1.4% with 5,16-androstadien-3β-ol (andien-β). The standard curve plotted as log picogram (pg) unlabelled 5α-androstenone against counts per minute (cpm) bound radioactive steroid was almost linear from 50 to 800 pg 5α-androstenone. Regression analysis of the data from the accuracy study gave the curve y = 0.99 x+ 203. The precision and sensitivity of the method were satisfactory. In plasma samples from sows and castrated male pigs the mean 5α-androstenone found was 1.1 ng/ml. In plasma samples from boars from 1.2 to 54.1 ng/ml was found.

scholarly journals Bovine Serum Albumin-Loaded Chitosan/Dextran Nanoparticles: Preparation and Evaluation ofEx VivoColloidal Stability in Serum

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Haliza Katas ◽  
Zahid Hussain ◽  
Siti Asarida Awang
Keyword(s):  
Particle Size ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Colloidal Stability ◽  
Ex Vivo ◽  
Biological Fluids ◽  
Chitosan Nanoparticles ◽  
Physiological Model

Chitosan (CS) nanoparticles have several distinct intrinsic advantages; however, theirin vivocolloidal stability in biological fluids was not fully explored especially when carrying proteins. The present study aimed to investigate their colloidal stability using anex vivophysiological model of fetal bovine serum (FBS) and human serum (HS). The stability of bovine-serum-albumin (BSA-) loaded nanoparticles was relatively higher in FBS than that in HS. Particle size of unloaded and BSA-loaded nanoparticles was statistically unchanged up to 24 h after incubation in FBS. However in HS, a significant increase in particle size from 144 ± 17 to 711 ± 22 nm was observed for unloaded nanoparticles and by 2.5-fold for BSA-loaded nanoparticle, at 24 h after incubation in HS. Zeta potential of both nanoparticles was less affected by the components in FBS compared to those in HS. A remarkable swelling extent was experienced for unloaded and BSA-loaded nanoparticles in HS, up to 54 ± 4% and 44 ± 5%, respectively. Morphology of unloaded and BSA-loaded nanoparticles was varied from smooth spherical and rod shape to irregular shape when incubated in FBS; however, form agglomerates when incubated in HS. These findings therefore suggest that HS is more reactive to cause colloidal instability to the chitosan nanoparticles compared to FBS.

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

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.

Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson
Keyword(s):  
Platelet Aggregation ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protective Effect ◽  
Whole Blood ◽  
Bovine Serum ◽  
Fatty Acid Content ◽  
Krebs Solution ◽  
Antiaggregatory Activity ◽  
Free Plasma

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.

RADIOIMMUNOASSAY OF OESTRONE AND OESTRADIOL IN THE PERIPHERAL PLASMA OF THE DOMESTIC FOWL IN VARIOUS PHYSIOLOGICAL STATES AND OF HYPOPHYSECTOMIZED AND OVARIECTOMIZED FOWLS

1974 ◽  
Vol 75 (1) ◽  
pp. 133-140 ◽  
Author(s):  
B. E. Senior
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Diethyl Ether ◽  
Bovine Serum ◽  
Domestic Fowl ◽  
Laying Hens ◽  
Peripheral Plasma ◽  
The Mean ◽  
Precision And Accuracy ◽  
Chicken Ovary

ABSTRACT A radioimmunoassay was developed to measure the levels of oestrone and oestradiol in 0.5–1.0 ml of domestic fowl peripheral plasma. The oestrogens were extracted with diethyl ether, chromatographed on columns of Sephadex LH-20 and assayed with an antiserum prepared against oestradiol-17β-succinyl-bovine serum albumin using a 17 h incubation at 4°C. The specificity, sensitivity, precision and accuracy of the assays were satisfactory. Oestrogen concentrations were determined in the plasma of birds in various reproductive states. In laying hens the ranges of oestrone and oestradiol were 12–190 pg/ml and 29–327 pg/ml respectively. Levels in immature birds, in adult cockerels and in an ovariectomized hen were barely detectable. The mean concentrations of oestrone and oestradiol in the plasma of four non-laying hens (55 pg/ml and 72 pg/ml respectively) and one partially ovariectomized hen (71 pg/ml and 134 pg/ml respectively) were well within the range for laying hens. It is evident that the large, yolk-filled follicles are not the only source of oestrogens in the chicken ovary.

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