81 An attempt to cyanylate the the thiol group of Bovine Serum Albumin with 13C-enriched cyanide and to observe the thiocyanate carbon by 13C-NMR

1998 ◽  
Vol 26 (1) ◽  
pp. S68-S68
Author(s):  
Declan A. Healy ◽  
Marrita M. Mahon ◽  
J. Paul G. Malthouse
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
13C Nmr ◽  
Bovine Serum ◽  
Thiol Group

scholarly journals Interactions of myristic acid with bovine serum albumin: a 13C NMR study.

1984 ◽  
Vol 81 (12) ◽  
pp. 3718-3722 ◽  
Author(s):  
J. A. Hamilton ◽  
D. P. Cistola ◽  
J. D. Morrisett ◽  
J. T. Sparrow ◽  
D. M. Small
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
13C Nmr ◽  
Myristic Acid ◽  
Bovine Serum ◽  
Nmr Study

scholarly journals Interactions of the carboxyl group of oleic acid with bovine serum albumin: a 13C NMR study.

1983 ◽  
Vol 258 (15) ◽  
pp. 9262-9269 ◽  
Author(s):  
J S Parks ◽  
D P Cistola ◽  
D M Small ◽  
J A Hamilton
Keyword(s):  
Oleic Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
13C Nmr ◽  
Bovine Serum ◽  
Carboxyl Group ◽  
Nmr Study

scholarly journals o-Quinones formed in plant extracts. Their reaction with bovine serum albumin

1969 ◽  
Vol 112 (5) ◽  
pp. 619-629 ◽  
Author(s):  
W. S. Pierpoint
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Plant Extracts ◽  
Bovine Serum ◽  
Succinic Anhydride ◽  
Thiol Group ◽  
Excess Oxygen ◽  
Amino Group ◽  
Amino Groups ◽  
Ellman's Reagent

1. The reactions between chlorogenoquinone, the o-quinone formed during the oxidation of chlorogenic acid, and bovine serum albumin depend on the ratio of reactants. 2. When the serum albumin is in excess, oxygen is not absorbed and the products are colourless. This reaction probably involves the thiol group of bovine serum albumin; it does not occur with bovine serum albumin which has been treated with p-chloromercuribenzoate, iodoacetamide or Ellman's reagent. 3. When bovine serum albumin reacts with excess of chlorogenoquinone, oxygen is absorbed and the products are red. The red colour is probably formed by reaction of the lysine ∈-amino groups of bovine serum albumin, as it is prevented by treating the protein with formaldehyde, succinic anhydride or O-methylisourea. 4. Bovine serum albumin modified by a 1·5-fold (BSA-Q) and a fivefold (BSA-Q2) excess of chlorogenoquinone were separated by chromatography on DEAE-Sephadex A-50, and some of their properties observed. 5. Reaction of BSA-Q2 with fluorodinitrobenzene suggests that the terminal α-amino group, as well as lysine ∈-amino groups, are combined with chlorogenoquinone.

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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