Polarographic catalytic wave of hydrogen ??Parallel catalytic hydrogen wave of bovine serum albumin in the presence of oxidants

2002 ◽  
Vol 45 (2) ◽  
pp. 158 ◽  
Author(s):  
Wei GUO
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Catalytic Wave ◽  
Catalytic Hydrogen ◽  
Polarographic Catalytic Wave

Effect of temperature on catalytic hydrogen currents of native and modified bovine serum albumin

1980 ◽  
Vol 45 (3) ◽  
pp. 669-678 ◽  
Author(s):  
Izaak Maurits Kolthoff ◽  
S. Kihara
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Temperature Effect ◽  
Bovine Serum ◽  
Effect Of Temperature ◽  
Catalytic Current ◽  
Catalytic Hydrogen ◽  
Increasing Temperature ◽  
Abnormal Temperature

The effect of temperature has been studied on three different catalytic hydrogen currents observed voltammetrically and on two of them polarographically with serum albumin and modified products of albumin adsorbed on mercury. The so-called "active cobalt catalytic current", ic and "presodium current", ips increase with increasing temperature. The temperature effect on the so-called Brdi_ka currents. i1 and i2 was found to be quite different from that on ic or ips. In ammoniacal buffer (pH = 9.3) in the presence of cobalt(III) or (II) i1 has been found virtually the same at temperature between 4° and 40°C, whereas i2 greatly decreases with increasing temperature. Evidence has been presented that in the presence of Co(III) or Co(II) and at 4°C all disulfide groups in the protein used are reduced to sulfhydryl at potentials at which i1 and i2 are observed. It has been concluded that the ligands of the protein which complex with Co(III) or Co(II) or Co(0) are different at potentials at which i1 is observed than at which i2 is observed. In order to account for the abnormal temperature effect on i2 it has been proposed that the area of the section of protein which is the seat of i2 is being detached from the surface with increasing temperature and that this process is reversible.

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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