Effect of (E,E)‐2,4‐decadienal on Side‐chain Modification, Conformation Change, and Aggregation of Bovine Serum Albumin

2021 ◽  
pp. 2100066
Author(s):  
Wenjuan Li ◽  
Yan Wu ◽  
Conghu Li ◽  
Liangliang Zhu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Side Chain ◽  
Conformation Change

scholarly journals Effect of alkyl distribution in pyrazine on pyrazine flavor release in bovine serum albumin solution

RSC Advances ◽  
2019 ◽  
Vol 9 (63) ◽  
pp. 36951-36959 ◽  
Author(s):  
Yun-Jiao Ma ◽  
Jian-Hai Wu ◽  
Xiang Li ◽  
Xian-Bing Xu ◽  
Zhen-Yu Wang ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Methyl Groups ◽  
Bovine Serum Albumin Solution ◽  
Conformation Change ◽  
Albumin Solution ◽  
Pyrazine Ring ◽  
Covalent Interaction ◽  
Flavor Release

The methyl groups on the pyrazine ring affect the interaction of pyrazines with BSA. The non-covalent interaction between alkyl-pyrazines and BSA was confirmed. Alkyl-pyrazines could induce the polarity and conformation change of BSA.

Association of Near-Infrared Dyes with Bovine Serum Albumin

1997 ◽  
Vol 51 (10) ◽  
pp. 1511-1515 ◽  
Author(s):  
Alkis J. Sophianopoulos ◽  
Jacek Lipowski ◽  
Narasimhachari Narayanan ◽  
Gabor Patonay
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Near Infrared ◽  
Association Constants ◽  
Molar Ratio ◽  
Side Chain ◽  
Optical Parameters ◽  
Hydrophobic Region ◽  
Near Ir

The binding of five near-infrared (near-IR) dyes to bovine serum albumin (BSA) has been evaluated by absorption, fluorescence, and circular dichroism. These dyes have a common squarilic acid polymethine backbone but differ in the substituents on two sites, R1 and R2, symmetrically located on the chromophore. The magnitude of the association constants for the dye–albumin complexes depended on the nature of the side chains and ranged from 34,000 to 1 × 107 M−1. Listed by the kind of side chain and in increasing binding order, the association constants are: [R1 = R2 = butyl phthalimide] < [R1 = R2 = cetyl] < [R1 = R2 = ethyl] < [R1 = butyl phthalimide, R2 = butyl sulfonate] < [R1 = R2 = butyl sulfonate]. The chromophore seems to interact mainly with a hydrophobic cavity on BSA. However, the association constants increase substantially when the side chain or chains are butyl sulfonate. This observation suggests that near the hydrophobic region there is at least one positively charged site with which the butyl sulfonate chain or chains interact. The molar ratio of the dye–albumin complex determined was 1:1. The optical constants of the dye–albumin complexes cannot be determined directly; therefore, a method is described for determining these complexes' optical parameters and thus their association constants.

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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