scholarly journals Influence of blood proteins on biomedical analysis. II. Interaction of gliclazide with bovine serum albumin.

1981 ◽  
Vol 29 (2) ◽  
pp. 573-577 ◽  
Author(s):  
KUNIO KOBAYASHI ◽  
TAKAFUMI SAKOGUCHI ◽  
MASAKO KIMURA ◽  
YUKO KITANI ◽  
AKIRA MATSUOKA
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Blood Proteins ◽  
Biomedical Analysis

scholarly journals Influence of blood proteins on biomedical analysis. V. Effect of ethyl alcohol on gliclazide-binding with bovine serum albumin.

1982 ◽  
Vol 30 (3) ◽  
pp. 1077-1080
Author(s):  
KUNIO KOBAYASHI ◽  
MASAKO KIMURA ◽  
TAKAFUMI SAKOGUCHI ◽  
AYUMI HASE ◽  
AKIRA MATSUOKA
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Ethyl Alcohol ◽  
Bovine Serum ◽  
Blood Proteins ◽  
Biomedical Analysis

scholarly journals Influence of blood proteins on biomedical analysis. I. Interaction of xanthurenic acid with bovine serum albumin.

1980 ◽  
Vol 28 (10) ◽  
pp. 2960-2966 ◽  
Author(s):  
KUNIO KOBAYASHI ◽  
TAKAFUMI SAKOGUCHI ◽  
MASAKO KIMURA ◽  
KUNIO HAITO ◽  
AKIRA MATSUOKA
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Xanthurenic Acid ◽  
Blood Proteins ◽  
Biomedical Analysis

Fibrinogen Adsorption on Hydroxyapatite, Carbonate Apatite and Gold Surfaces In Situ Detected by Quartz Crystal Microbalance with Resistance Technique

2012 ◽  
Vol 1418 ◽  
Author(s):  
Hiroshi Yonekura ◽  
Motohiro Tagaya ◽  
Tomohiko Yoshioka ◽  
Toshiyuki Ikoma ◽  
Junzo Tanaka
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Force ◽  
Gold Surface ◽  
The Body ◽  
Adsorption Behavior ◽  
Carbonate Apatite ◽  
Blood Proteins ◽  
Biomaterial Surfaces

ABSTRACTWhen a biomaterial is implanted into the body, blood proteins adsorb on its surface and subsequently cells adhere via the protein adlayer. Thus, the understanding of protein adsorption and conformational change on the biomaterial surfaces is of great importance to control the biocompatibility such as antithrombotic properties and cell adhesion behaviors. In this study, we synthesized hydroxyapatite (HAp) and carbonate apatite (CAp) by a wet method. Then we successfully fabricated the HAp and CAp sensors for QCM-R by an electrophoretic deposition method. Adsorption behavior of proteins on the bone substitute material can be monitored by using these apatite sensors. Bovine serum albumin and fibrinogen were employed for the model proteins, and monitored the adsorption behavior on the HAp, CAp and reference gold (Au) sensors by the QCM-R technique. As a result, we revealed that fibrinogen and bovine serum albumin adsorbs on the gold surface by hydrophobic interaction, and adsorbs on the HAp and CAp surfaces mainly by electrostatic force. Besides, we revealed that fibrinogen adsorbs on the Au surface more rigid than on the HAp and CAp surfaces while bovine serum albumin adsorbs on the HAp and CAp surface more rigidly than on the Au surface.

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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