Ubiquitin-dependent proteolysis of native and alkylated bovine serum albumin: effects of protein structure and ATP concentration on selectivity

Biochemistry ◽  
1985 ◽  
Vol 24 (12) ◽  
pp. 2915-2923 ◽  
Author(s):  
Anthony C. Evans ◽  
Keith D. Wilkinson
Keyword(s):  
Protein Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Atp Concentration

Adsorption of bovine serum albumin on gold nanoprisms: interaction and effect of NIR irradiation on protein corona

2020 ◽  
Vol 8 (37) ◽  
pp. 8644-8657
Author(s):  
Karen Bolaños ◽  
Freddy Celis ◽  
Carlos Garrido ◽  
Marcelo Campos ◽  
Fanny Guzmán ◽  
...  
Keyword(s):  
Protein Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conversion Efficiency ◽  
Bovine Serum ◽  
Protein Corona ◽  
Photothermal Conversion ◽  
Corona Formation ◽  
Gold Nanoprisms

The photothermal conversion efficiency of AuNPr–PEG after albumin corona formation and the effect of irradiation on the protein structure were evaluated.

scholarly journals pH DEPENDENT STRUCTURES OF BOVINE SERUM IN SOLUTION BY SMALL ANGLE NEUTRON SCATTERING

2021 ◽  
Vol 83 (2) ◽  
pp. 117-123
Author(s):  
Arum Patriati ◽  
Edy Giri Rachman Putra
Keyword(s):  
Crystal Structure ◽  
Protein Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Neutron Scattering ◽  
Small Angle ◽  
Bovine Serum ◽  
Small Angle Neutron Scattering ◽  
Static State ◽  
Ph Dependent

The pH-dependent structures of the bovine serum albumin (BSA), under physiological conditions that permit enzymatic activity, were investigated by small-angle neutron scattering (SANS). The unfolding behavior of BSA in solution is important to understand the mechanism of protein aggregation due to protein conformational change. The information of protein structure is crucial to design the perfect protein-based drug delivery device. This information will be useful as a complementary data of BSA crystal structure in static state. The structure of BSA in solution was found to be heart shaped, nearly identical to bovine serum albumin crystal structure. The globular heart shaped structure of BSA was still maintained at alkaline pH range of 7 to 11. It underwent partial unfolding at pH 5 and continued to unfold at pH 3. The unfolded-structure of BSA shows that the globular structure started to change into a cylinder-like structure at pH 3 which was clearly shown in Kratky plot. These results were confirmed with ab initio low-resolution shape calculation model analysis using GNOM and DAMMIF in obtaining the three-dimensional protein structure model.

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.

Sign in / Sign up

Export Citation Format

Share Document