Adsorption of Bovine Serum and Bovine Haemoglobin onto Chitosan Film

The technique of labeling of macromolecules with ferritin conjugated antibody has been successfully used for extracellular antigen by means of staining the specimen with conjugate prior to fixation and embedding. However, the ideal method to determine the location of intracellular antigen would be to do the antigen-antibody reaction in thin sections. This technique contains inherent problems such as the destruction of antigenic determinants during fixation or embedding and the non-specific attachment of conjugate to the embedding media. Certain embedding media such as polyampholytes (2) or cross-linked bovine serum albumin (3) have been introduced to overcome some of these problems.

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Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100128122 ◽

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.

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Albumin-Induced Endocytic Vacuoles in Tetrahymena Pyrijormis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100117091 ◽

1975 ◽

Vol 33 ◽

pp. 694-695

Author(s):

L. J. Brenner ◽

D. G. Osborne ◽

B. L. Schumaker

Keyword(s):

Electron Microscopy ◽

Bovine Serum Albumin ◽

Bovine Serum ◽

Protein Concentration ◽

Tetrahymena Pyriformis ◽

Sequence Of Events ◽

Cytoplasmic Bodies ◽

Food Vacuoles ◽

Mouse Ascites ◽

Normal Human

Exposure of the ciliate, Tetrahymena pyriformis, strain WH6, to normal human or rabbit sera or mouse ascites fluids induces the formation of large cytoplasmic bodies. By electron microscopy these (LB) are observed to be membrane-bounded structures, generally spherical and varying in size (Fig. 1), which do not resemble the food vacuoles of cells grown in proteinaceous broth. The possibility exists that the large bodies represent endocytic vacuoles containing material concentrated from the highly nutritive proteins and lipoproteins of the sera or ascites fluids. Tetrahymena mixed with bovine serum albumin or ovalbumin solutions having about the same protein concentration (7g/100 ml) as serum form endocytic vacuoles which bear little resemblance to the serum-induced LB. The albumin-induced structures (Fig. 2) are irregular in shape, rarely spherical, and have contents which vary in density and consistency. In this paper an attempt is made to formulate the sequence of events which might occur in the formation of the albumin-induced vacuoles.

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The adsorption of bovine serum albumin at the stainless-steel/aqueous solution interface

Journal of Colloid and Interface Science ◽

10.1016/s0021-9797(84)80018-1 ◽

1984 ◽

Vol 98 (1) ◽

pp. 138-143 ◽

Cited By ~ 4

Author(s):

H VANENCKEVORT ◽

D DASS ◽

A LANGDON

Keyword(s):

Aqueous Solution ◽

Stainless Steel ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Solution Interface

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Fibrinogen and its Derivatives: Cofactors in the Intrinsic Generation of Thrombin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1647923 ◽

1976 ◽

Vol 35 (02) ◽

pp. 305-313 ◽

Cited By ~ 1

Author(s):

D.C Triantaphyllopoulos ◽

L.T Ryan

Keyword(s):

Factor Viii ◽

Vitamin K ◽

Bovine Serum ◽

Thrombin Generation ◽

Factor V ◽

Simultaneous Addition ◽

Lower Effect

SummaryThe simultaneous addition of suboptimal concentrations of factor VIII and intact or plas-min-lysed fibrinogen into mixtures of the vitamin K dependent factors, phospholipids, adsorbed bovine serum (supplier of factor V) and calcium, increased the amount of thrombin which was generated three to twenty times over the sum of the amounts which were generated when factor VIII, or fibrinogen, or its derivatives were added separately into the thrombin generating mixture. When factor VIII was added together with both fibrinogen and its derivatives, the amount of thrombin generated was even greater, about 130% larger than the amount which was generated in the presence of equal concentrations of only intact fibrinogen plus factor VIII. Addition of albumin instead of fibrinogen or its derivatives has a similar but significantly lower effect on thrombin generation. It appears, therefore, that both intact fibrinogen and its plasminolytic derivatives, singly or in combination, and to a lesser extent albumin, act as cofactors in the reaction which is regulated by factor VIII.

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Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653438 ◽

1981 ◽

Vol 46 (03) ◽

pp. 645-647 ◽

Cited By ~ 28

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.

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Inactivation of Antiplasmin and Complement C1 in Human Plasma Rendered Fibrinolytic by Synthetic Organic Compounds

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654771 ◽

1963 ◽

Vol 10 (01) ◽

pp. 151-163 ◽

Cited By ~ 2

Author(s):

Kurt N von Kaulla

Keyword(s):

Human Plasma ◽

Organic Compounds ◽

Bovine Serum ◽

Fibrinolytic Activity ◽

Plasma Generation ◽

Synthetic Organic Compounds

SummaryCertain synthetic organic compounds induce upon dissolution marked fibrinolytic activity in human plasma, reduce the antiplasmin titer of human or bovine serum and destroy the complement C1 of human plasma. Generation of fibrinolytic activity and reduction of antiplasmin are concentration-depending time reactions. Destruction of complement C1 occurs almost instantaneously. Minor molecular modifications abolish all three activities of the compounds.

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Bovine Platelet Proteins

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653555 ◽

1969 ◽

Vol 21 (03) ◽

pp. 409-418 ◽

Cited By ~ 2

Author(s):

S Łopaciuk ◽

N. O Solum

Keyword(s):

Bovine Serum ◽

Protein Composition ◽

Disc Electrophoresis ◽

Plasma Fibrinogen ◽

Plasma Albumin ◽

Precipitin Line ◽

Bovine Plasma ◽

Platelet Proteins

Summary1. The protein composition of bovine platelet extracts has been investigated by immunoelectrophoresis and polyacrylamide disc electrophoresis. The information obtained is discussed as a basis for study on platelet fibrinogen.2. With antiserum to platelet proteins 11 precipitin lines were observed 3 of which corresponded electrophoretically to plasma albumin, fibrinogen and γ-globulin. These lines were not seen using the same antiserum absorbed with bovine plasma. The 8 additional lines were still present indicating that they represented specific platelet components. Antiserum to plasma produced the 3 above-mentioned lines, but no others.3. With antiserum to purified bovine plasma fibrinogen 3 precipitin lines were observed. The fibrinogen line was the dominant one. The 2 additional lines did not disappear by absorption of the antiserum with bovine serum nor by incubation of the extracts with thrombin. The latter treatment totally removed the fibrinogen line.4. A non-fibrinogen precipitin line, observed only with the antiserum to platelet extract and positioned in the β2-globulin region, disappeared by the incubation of platelet extracts with thrombin.

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RADIOIMMUNOASSAY OF OESTRONE AND OESTRADIOL IN THE PERIPHERAL PLASMA OF THE DOMESTIC FOWL IN VARIOUS PHYSIOLOGICAL STATES AND OF HYPOPHYSECTOMIZED AND OVARIECTOMIZED FOWLS

Acta Endocrinologica ◽

10.1530/acta.0.0750133 ◽

1974 ◽

Vol 75 (1) ◽

pp. 133-140 ◽

Cited By ~ 9

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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