Factors Affecting the Primary and Secondary Responses to Bovine Serum Albumin in Chickens

1965 ◽  
Vol 26 (2) ◽  
pp. 80-95 ◽  
Author(s):  
A.A. Blazkovec ◽  
H.R. Wolfe
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Factors Affecting

Sonochemically prepared bovine serum albumin microcapsules: factors affecting the size distribution and the microencapsulation yield

2001 ◽  
Vol 22 (3) ◽  
pp. 251-255 ◽  
Author(s):  
Kimiko Makino ◽  
Taro Mizorogi ◽  
Shizutoshi Ando ◽  
Takeyo Tsukamoto ◽  
Hiroyuki Ohshima
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Size Distribution ◽  
Bovine Serum ◽  
Factors Affecting

Reverse Micelle Liquid-Liquid Extraction of Bovine Serum Albumin and Lysozyme

2012 ◽  
pp. 07-11 ◽  
Author(s):  
Siti Hamidah Mohd Setapar ◽  
Siti Norazimah Mohamad Aziz ◽  
Constantine Joanne
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Reverse Micelle ◽  
Bovine Serum ◽  
Surfactant Concentration ◽  
Extraction Process ◽  
Factors Affecting ◽  
Forward Transfer ◽  
Protein Bovine Serum Albumin ◽  
Reverse Micelle Extraction

Reverse micelle extraction by using Sodium bis (2-ethylhexyl) Suffoccinate (AOT) of protein bovine serum albumin (BSA) and lysozyme was investigated in this research. Study of factors affecting the surfactant concentration and pH of aqueous for both forward and backward extraction process was performed in the research. The BSA concentrations were characterized by using the UV- spectrophotometer at wavelength, λ = 280 nm. The result indicated that the extraction percentage of lysozyme was higher than BSA in forward transfer for both parameters; however BSA demonstrated a better extraction performance in backward extraction process. The maximum lysozyme extracted in the forward extraction process was at 60 mM of surfactant concentration while for BSA was 100 mM since BSA is a bulky molecule and the size is larger than of lysozyme. Pengekstrakan misel terbalik dengan menggunakan Sodium bis (2-ethylhexyl) Suffoccinate (AOT) untuk protein bovine serum albumin (BSA) dan lysozyme disiasat dalam penyelidikan ini. Kajian tentang faktor-faktor yang mempengaruhi kepekatan surfaktan dan pH akueus untuk proses pengekstrakan hadapan dan ke belakang telah dijalankan. Kepekatan BSA telah dicirikan dengan menggunakan spektrofotometer UV pada panjang gelombang, λ = 280 nm. Hasil kajian telah menunjukkan bahawa peratusan pengekstrakan lysozyme adalah lebih tinggi daripada BSA bagi pemindahan ke hadapan untuk kedua-dua parameter, namun begitu BSA menunjukkan prestasi pengekstrakan yang lebih baik di dalam proses pengekstrakan kebelakang. Jumlah maksimum lysozyme yang diekstrak di dalam proses pengekstrakan ke hadapan adalah 60 mM kepekatan surfaktan manakala bagi BSA adalah 100 mM disebabkan BSA adalah molekul yang sangat besar dan ia mempunyai saiz yang lebih besar berbanding daripada lysozyme.

Factors Affecting Heat-Induced Gel Formation of Bovine Serum Albumin

1986 ◽  
Vol 51 (5) ◽  
pp. 1289-1292 ◽  
Author(s):  
KUMI YASUDA ◽  
RYO NAKAMURA ◽  
SHIGERU HAYAKAWA
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Gel Formation ◽  
Factors Affecting

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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