Surface Functionalization of Porous Glass Networks:  Effects on Bovine Serum Albumin and Porcine Insulin Immobilization

2000 ◽  
Vol 1 (4) ◽  
pp. 789-797 ◽  
Author(s):  
Herman S. Mansur ◽  
Zélia P. Lobato ◽  
Rodrigo L. Oréfice ◽  
Wander L. Vasconcelos ◽  
Cintia Oliveira ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Functionalization ◽  
Porous Glass ◽  
Bovine Serum ◽  
Porcine Insulin

Partitioning of whey proteins, bovine serum albumin and porcine insulin in aqueous two-phase systems

2000 ◽  
Vol 743 (1-2) ◽  
pp. 235-239 ◽  
Author(s):  
José G.L.F Alves ◽  
Lucy D.A Chumpitaz ◽  
Luiza H.M da Silva ◽  
Telma T Franco ◽  
Antonio J.A Meirelles
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Whey Proteins ◽  
Porcine Insulin ◽  
Two Phase ◽  
Aqueous Two Phase Systems ◽  
Phase Systems

scholarly journals Development of Poly(2-Methacryloyloxyethyl Phosphorylcholine)-Functionalized Hydrogels for Reducing Protein and Bacterial Adsorption

Materials ◽  
2020 ◽  
Vol 13 (4) ◽  
pp. 943 ◽  
Author(s):  
Temmy Pegarro Vales ◽  
Jun-Pil Jee ◽  
Won Young Lee ◽  
Sung Cho ◽  
Gye Myung Lee ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Functionalization ◽  
Bovine Serum ◽  
High Water ◽  
High Water Content ◽  
Hydroxyethyl Methacrylate ◽  
Zwitterionic Polymer ◽  
Bacterial Adsorption ◽  
Enhanced Surface

A series of hydrogels with intrinsic antifouling properties was prepared via surface-functionalization of poly(2-hydroxyethyl methacrylate) [p(HEMA)]-based hydrogels with the biomembrane-mimicking zwitterionic polymer, poly(2-methacryloyloxyethyl phosphorylcholine) [p(MPC)]. The p(MPC)-modified hydrogels have enhanced surface wettability, high water content retention (61.0%–68.3%), and good transmittance (>90%). Notably, the presence of zwitterionic MPC moieties at the hydrogel surfaces lowered the adsorption of proteins such as lysozyme and bovine serum albumin (BSA) by 73%–74% and 59%–66%, respectively, and reduced bacterial adsorption by approximately 10%–73% relative to the unmodified control. The anti-biofouling properties of the p(MPC)-functionalized hydrogels are largely attributed to the dense hydration layer formed at the hydrogel surfaces by the zwitterionic moieties. Overall, the results demonstrate that biocompatible and antifouling hydrogels based on p(HEMA)-p(MPC) structures have promising potential for application in biomedical materials.

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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