Development of bovine serum albumin-water partition coefficients predictive models for ionogenic organic chemicals based on chemical form adjusted descriptors

2017 ◽  
Vol 144 ◽  
pp. 131-137 ◽  
Author(s):  
Feng Ding ◽  
Xianhai Yang ◽  
Guosong Chen ◽  
Jining Liu ◽  
Lili Shi ◽  
...  
2019 ◽  
Vol 21 (11) ◽  
pp. 1852-1863 ◽  
Author(s):  
Flora Allendorf ◽  
Urs Berger ◽  
Kai-Uwe Goss ◽  
Nadin Ulrich

Alternatives to long-chain PFAAs sorb similarly strongly to serum albumin as the classical PFAAs.


1970 ◽  
Vol 116 (2) ◽  
pp. 171-175 ◽  
Author(s):  
A. G. Ogston ◽  
Panee Silpananta

1. We have measured the partition coefficients of bovine serum albumin with Sephadex grades G-100, G-150 and G-200, and of a dextran ([unk]n 19700) and a polyethylene glycol ([unk]n 8000) with Sephadex G-200. We have also measured the effects of these solutes on the inner volumes of the grades of Sephadex. 2. The results can be described with fair consistency by means of a simple thermodynamic treatment that makes use of the virial coefficients of Sephadex and of the solute, and of a coefficient that expresses their interaction. This coefficient is related to the ‘exclusion volume’ of Sephadex for the solutes. 3. The Sephadex G-200–polyethylene glycol system shows anomalies of behaviour that are ascribed to the occurrence of ‘incompatible’ phase separation within the Sephadex beads.


2017 ◽  
Vol 19 (3) ◽  
pp. 261-269 ◽  
Author(s):  
Lukas Linden ◽  
Kai-Uwe Goss ◽  
Satoshi Endo

The 3D-QSAR model predicts the bovine serum albumin–water partition coefficients for neutral and anionic chemicals influenced by steric effects.


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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