scholarly journals Interactions between Orange II and Components in Heat-Treated Bovine Serum Albumin

1982 ◽  
Vol 31 (12) ◽  
pp. 988-992
Author(s):  
Koichiro AOKI ◽  
Koji ONDA ◽  
Shuji OKUMURA ◽  
Mamoru MURATA ◽  
Koichi HIRAMATSU
2000 ◽  
Vol 14 (2) ◽  
pp. 95-110 ◽  
Author(s):  
S Neiser ◽  
K.I Draget ◽  
O Smidsrød

1998 ◽  
Vol 12 (2) ◽  
pp. 127-132 ◽  
Author(s):  
Susann Neiser ◽  
Kurt I. Draget ◽  
Olav Smidsrød

2001 ◽  
Vol 64 (1) ◽  
pp. 108-112 ◽  
Author(s):  
HIROMI URANO ◽  
SATOSHI FUKUZAKI

Facilitation of cleaning of alumina (Al2O3) particles fouled with heat-treated bovine serum albumin (BSA), which contains sulfhydryl groups on the molecule, by gaseous ozone was studied. With increasing temperature of heat treatment, the amount of adsorbed BSA onto Al2O3 surfaces increased, whereas the rate of BSA desorption during alkali cleaning decreased markedly, resulting in the larger amounts of BSA remaining on Al2O3 surfaces. No significant amounts of BSA were removed from Al2O3 surfaces by alkali cleaning alone when treated at temperatures above 120°C. Before alkali cleaning, the heat-treated, BSA-fouled Al2O3 at 150°C were treated with 0.05 to 0.30% (vol/vol) gaseous ozone at room temperature. Ozone pretreatment markedly accelerated the rate of BSA desorption during subsequent alkali cleaning. The effect of ozone pretreatment on BSA removal depended on the concentration of ozone and treatment time and hence on the total amount of ozone supplied. The molecular weight (MW) of desorbed BSA during alkali cleaning without ozone pretreatment coincided with the MW of the native BSA, whereas the MW of desorbed BSA during the combined ozone-alkali cleaning was lower than the MW of the native BSA. This indicated that the heat-treated BSA molecules adsorbed on Al2O3 were partially decomposed into some fragments by ozone pretreatment, resulting in the facilitation of the removal of BSA during alkali cleaning.


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.


1974 ◽  
Vol 75 (1) ◽  
pp. 133-140 ◽  
Author(s):  
B. E. Senior

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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