The antigenic structure of bovine serum albumin. Evidence for multiple, different, domain-specific antigenic determinants.

The technique of labeling of macromolecules with ferritin conjugated antibody has been successfully used for extracellular antigen by means of staining the specimen with conjugate prior to fixation and embedding. However, the ideal method to determine the location of intracellular antigen would be to do the antigen-antibody reaction in thin sections. This technique contains inherent problems such as the destruction of antigenic determinants during fixation or embedding and the non-specific attachment of conjugate to the embedding media. Certain embedding media such as polyampholytes (2) or cross-linked bovine serum albumin (3) have been introduced to overcome some of these problems.

Download Full-text

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100128122 ◽

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.

Download Full-text

The adsorption of bovine serum albumin at the stainless-steel/aqueous solution interface

Journal of Colloid and Interface Science ◽

10.1016/s0021-9797(84)80018-1 ◽

1984 ◽

Vol 98 (1) ◽

pp. 138-143 ◽

Cited By ~ 4

Author(s):

H VANENCKEVORT ◽

D DASS ◽

A LANGDON

Keyword(s):

Aqueous Solution ◽

Stainless Steel ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Solution Interface

Download Full-text

Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653438 ◽

1981 ◽

Vol 46 (03) ◽

pp. 645-647 ◽

Cited By ~ 28

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.

Download Full-text