Etude d'interactions moléculaires en solution par analyse de la relaxation quadripolaire du deutérium. II. Associations de l'albumine sérique de bœuf en solution aqueuse

1981 ◽  
Vol 59 (12) ◽  
pp. 1701-1704 ◽  
Author(s):  
Yves Van Haverbeke ◽  
André Maquestiau ◽  
Robert Muller ◽  
Luce Vander Elst
Keyword(s):  
Relaxation Time ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Relaxation Rate ◽  
Bovine Serum ◽  
Longitudinal Relaxation Time ◽  
Ph Profile ◽  
Longitudinal Relaxation ◽  
Solution Aqueuse

Deuterium longitudinal relaxation time is used for assessing the interaction between bovine serum albumin (BSA) and some drugs. The study of unenriched compounds by means of a reference equilibrium is successfully applied.The deuterium relaxation rate of pyridine versus the pH profile allows a better understanding of the nature of the interactions. Some experimental aspects are discussed.

Bewegungen der CH3-Gruppen in Methyl-Naphtalin-Kristallen .III.Protonenspin-Relaxation bei tiefen Temperaturen / Rotation of CH3 Croups in Methyl Naphthalene Crystals at low Temperatures

1973 ◽  
Vol 28 (1) ◽  
pp. 69-76 ◽  
Author(s):  
J. U. von Schütz ◽  
W. Güttler ◽  
H. C. Wolf
Keyword(s):  
Relaxation Time ◽  
Relaxation Rate ◽  
Low Temperatures ◽  
Methyl Groups ◽  
Longitudinal Relaxation Time ◽  
Kcal Mole ◽  
Temperature Range ◽  
Longitudinal Relaxation ◽  
Comparison Of The Results ◽  
Methyl Naphthalene

In continuation of earlier works (temperature range 400 - 77 K) the temperature and frequency dependencies of the longitudinal relaxation time T1 in different methyl naphthalene crystals were measured down to 4,2 K at 22 and 56 MHz. The observation of two minima in some cases below 50 K could be attributed quantitatively to the weakly hindered β-CH3 groups (EA <0,8 kcal/mole) by comparison of the results of similar methyl naphthalenes. The low relaxation rate in the minima is due to tunneling effects of the methyl groups. The splitting of the lowest torsional niveau could be roughly determined.

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