Comparison of whole body and tissue blood volumes in rainbow trout (Salmo gairdneri) with125I bovine serum albumin and51Cr-erythrocyte tracers

1989 ◽  
Vol 6 (1) ◽  
pp. 39-47 ◽  
Author(s):  
W. H. Gingerich ◽  
R. A. Pityer
Keyword(s):  
Rainbow Trout ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Whole Body ◽  
Salmo Gairdneri ◽  
Blood Volumes

Hyperosmotic Infiltration: Factors Influencing Uptake of Bovine Serum Albumin by Rainbow Trout (Salmo gairdneri)

1978 ◽  
Vol 35 (6) ◽  
pp. 871-874 ◽  
Author(s):  
D. C. Fender ◽  
D. F. Amend
Keyword(s):  
Rainbow Trout ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Osmotic Pressure ◽  
Bovine Serum ◽  
Immersion Time ◽  
Salmo Gairdneri ◽  
Nacl Solution ◽  
Step Method ◽  
Solution Ph

Infiltration of bovine serum albumin (BSA) into the blood of rainbow trout (Salmo gairdneri) by hyperosmotic infiltration (HI) was studied by varying the osmotic pressure, immersion time, pH, temperature, stress, vacuum, and fish size. Compared with uptake of BSA from water solutions, about 1400 mosM (4.51%) NaCl was required to increase the plasma level of BSA during a 3-min immersion. Higher osmotic pressures resulted in higher plasma-BSA levels, but the uptake of BSA was limited by the length of time that fish could tolerate the high NaCl concentration. Comparison of immersion time in the solutions of the two-step HI method showed that maximum infiltration occurred after a 2–3-min bath in the 5.32% NaCl solution and only 30 s in the 2% BSA solution. Alkaline solution (pH 9) enhanced BSA uptake in the one-step method, but the two-step method was most effective if the NaCl solution was pH 9 and the BSA solution pH 5. BSA uptake was directly proportional to water temperature from 4 to 20 °C. Preimmersion stress, and injection of 10 μg epinephrine, reduced BSA uptake; vacuum and fish weight (2–8 g) had no effect on uptake of BSA. Hyperosmotic infiltration may be useful for mass delivery of vaccines, pharmaceuticals, and other materials. Key words: hyperosmotic infiltration, bovine serum albumin, osmotic pressure, vaccines, immersion, rocket immunoelectrophoresis

Whole-body measurement of radioactivity as a means of following in vivo the degradation of I131-labeled proteins in mice

1960 ◽  
Vol 198 (6) ◽  
pp. 1355-1360 ◽  
Author(s):  
Geronimo Terres ◽  
W. L. Hughes ◽  
W. Wolins
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Trichloroacetic Acid ◽  
Whole Body ◽  
Body Measurements ◽  
Body Measurement ◽  
Serum Samples ◽  
Secular Equilibrium

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.

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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