SuFEx: a metal-free click ligation for multivalent biomolecules

In this work, we use a spontaneous and catalyst-free amino-yne click bioconjugation to generate activated ethynyl group functionalized surfaces for fast immobilizing native proteins and cells. Biomolecules, such as bovine serum albumin (BSA), human IgG and peptide of C(RGDfK), could be covalently immobilized on the surfaces in as short as 30 min. Notably, the bioactivity of the anchored biomolecules remain intact, which is verified by efficiently capturing target antibodies and cells from the bulk solutions. This strategy represents an alternative for highly efficient surface biofunctionalization.

Download Full-text

Fast Surface Immobilization of Native Proteins through Metal-Free Amino-yne Click Bioconjugation

10.26434/chemrxiv.10303412 ◽

2019 ◽

Author(s):

Yiru Zhang ◽

Jianlei Shen ◽

Rong Hu ◽

Shi Xiujuan ◽

Xianglong Hu ◽

...

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Free Amino ◽

Surface Immobilization ◽

Ethynyl Group ◽

Metal Free ◽

Native Proteins ◽

Functionalized Surfaces ◽

Bulk Solutions

In this work, we use a spontaneous and catalyst-free amino-yne click bioconjugation to generate activated ethynyl group functionalized surfaces for fast immobilizing native proteins and cells. Biomolecules, such as bovine serum albumin (BSA), human IgG and peptide of C(RGDfK), could be covalently immobilized on the surfaces in as short as 30 min. Notably, the bioactivity of the anchored biomolecules remain intact, which is verified by efficiently capturing target antibodies and cells from the bulk solutions. This strategy represents an alternative for highly efficient surface biofunctionalization.

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

RADIOIMMUNOASSAY OF OESTRONE AND OESTRADIOL IN THE PERIPHERAL PLASMA OF THE DOMESTIC FOWL IN VARIOUS PHYSIOLOGICAL STATES AND OF HYPOPHYSECTOMIZED AND OVARIECTOMIZED FOWLS

Acta Endocrinologica ◽

10.1530/acta.0.0750133 ◽

1974 ◽

Vol 75 (1) ◽

pp. 133-140 ◽

Cited By ~ 9

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.

Download Full-text