STUDIES ON BACTERIAL AGGLUTINATION BY USE OF THE ANTIGLOBULIN (COOMBS) TECHNIQUE

1956 ◽  
Vol 2 (7) ◽  
pp. 657-664 ◽  
Author(s):  
Arthur C. Ford ◽  
Ralph J. DeFalco
Keyword(s):  
Antibody Titer ◽  
Human Albumin ◽  
Bacterial Cells ◽  
Specific Test ◽  
Bovine Albumin ◽  
Cell Antigen ◽  
Antiglobulin Test ◽  
Bacterial Agglutination

The Coombs antiglobulin test has been successfully applied to bacterial cells in agglutination reactions. The test is a test for attached antibody globulin. Titers obtained by this method are shown to be from one to three tubes higher than those obtained by routine agglutination tests. Polyvinylpyrrolidone (PVP), bovine albumin, and human albumin have also been shown to hasten and strengthen bacterial agglutinations. The incomplete albumin reacting antibody titer of antisera seems to be higher than that of the saline reacting, or complete antibodies. The Coombs reaction is a specific test for antibody globulin attached to sensitized cells. There is no reaction where there is no combination between antibody globulin and the cell antigen, as shown by heterologous tests.

Bovine Albumin-Like Protein in Commercial Human Albumin for Clinical Use

Vox Sanguinis ◽  
1990 ◽  
Vol 59 (1) ◽  
pp. 1-5
Author(s):  
T. Murozuka ◽  
M. Moriwaka ◽  
H. Ito ◽  
S. Sekiguchi ◽  
M. Naiki ◽  
...  
Keyword(s):  
Human Albumin ◽  
Clinical Use ◽  
Bovine Albumin

A STUDY OF THE STORAGE STABILITY OF VIRAL ANTISERA

1965 ◽  
Vol 11 (3) ◽  
pp. 503-507 ◽  
Author(s):  
F. P. Nagler ◽  
J. R. Polley
Keyword(s):  
Antibody Titer ◽  
Diagnostic Tests ◽  
Storage Stability ◽  
High Titer ◽  
Bovine Albumin ◽  
The Stability

Antisera prepared against certain viruses contained antibodies of particularly high titer and it seemed desirable to dilute them before distribution for use in diagnostic tests. A study was made of the stability of viral antisera stored undiluted and diluted under various conditions. It was found that, in general, the sera could be diluted, lyophilized, and stored, even at 37 °C for a year, with little or no loss of antibody titer if the diluent was 5% peptone or 10% bovine albumin rather than saline.

Bovine Albumin-Like Protein in Commercial Human Albumin for Clinical Use

Vox Sanguinis ◽  
1990 ◽  
Vol 59 (1) ◽  
pp. 1-5 ◽  
Author(s):  
T. Murozuka ◽  
M. Moriwaka ◽  
H. Ito ◽  
S. Sekiguchi ◽  
M. Naiki ◽  
...  
Keyword(s):  
Human Albumin ◽  
Clinical Use ◽  
Bovine Albumin

Paper-based assay for red blood cell antigen typing by the indirect antiglobulin test

2016 ◽  
Vol 408 (19) ◽  
pp. 5231-5238 ◽  
Author(s):  
Natasha Yeow ◽  
Heather McLiesh ◽  
Liyun Guan ◽  
Wei Shen ◽  
Gil Garnier
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Cell Antigen ◽  
Indirect Antiglobulin Test ◽  
Antiglobulin Test

THE pH DEPENDENCE OF THE ADSORPTION ISOTHERM AND ABSORPTION SPECTRUM OF METHYL ORANGE BOUND TO HUMAN AND BOVINE SERUM ALBUMIN

1953 ◽  
Vol 31 (8) ◽  
pp. 734-745 ◽  
Author(s):  
J. Ross Colvin
Keyword(s):  
Methyl Orange ◽  
Binding Sites ◽  
Binding Capacity ◽  
Ph Dependence ◽  
Human Albumin ◽  
Electrostatic Repulsion ◽  
Bovine Albumin ◽  
Appreciable Increase ◽  
Protein Molecules ◽  
The Difference

The difference between adsorption isotherms and absorption spectra of methyl orange bound to human and to bovine albumin at pH 6.8, 9.1, and 11.0 has been studied. Exaltation of the spectrum of methyl orange bound to human albumin is not necessarily correlated with total binding capacity. However, above pH 6.8, heterogeneity of the binding sites for methyl orange on human albumin increases so markedly that it is reflected in an appreciable increase in extinction coefficient for the first three or four anions bound. The exaltation is accompanied by an increased −ΔF° of binding. Increase in ionic strength diminishes exaltation, and denaturation of the protein destroys it. These effects were not observed for bovine albumin. Results are interpreted in terms of a limited reversible expansion of the human protein molecules, without unfolding, due to intramolecular, electrostatic repulsion between groups.

Diversity of IgG Antibody Responses in the Patients with Various Types of Periodontitis

1988 ◽  
Vol 2 (2) ◽  
pp. 334-338 ◽  
Author(s):  
I. Ishikawa ◽  
H. Watanabe ◽  
M. Horibe ◽  
Y. Izumi
Keyword(s):  
Bone Loss ◽  
Antibody Titer ◽  
Fusobacterium Nucleatum ◽  
Enzyme Linked Immunosorbent Assay ◽  
Bacterial Cells ◽  
Bacterial Strains ◽  
Igg Antibody ◽  
Periodontopathic Bacteria ◽  
Healthy Control ◽  
Bacteroides Gingivalis

Serum IgG antibodies to seven periodontopathic bacteria were assessed with an enzyme-linked immunosorbent assay (ELISA) in 56 patients with periodontitis. Patients were selected according to the severity of bone loss, and were also classified into three categories by age: juvenile periodontitis (JP), advanced destructive periodontitis (ADP), and adult periodontitis (AP). Bacteroides gingivalis, B. loescheii, Fusobacterium nucleatum, Actinobacillus actinomycetemcomitans, Eikenella corrodens, B. intermedius, and Capnocytophaga ochracea were the bacterial strains of interest. Antigens were prepared by cold ultrasonication of washed bacterial cells. Association of high- or low-IgG antibody titer to the bacteria was evaluated. High or low titers of IgG were based on ELISA measurements in 28 healthy subjects. Values exceeding 100% above or below the normal standard deviation were classified as high or low titers, respectively. Most patients with three types of periodontitis (76.8%) exhibited high-IgG antibody titers against various periodontopathic bacteria. The sera mostly included high-IgG titer against one or some of B. gingivalis, E. corrodens, F. nucleatum, and/or A. actinomycetemcomitans. B. gingivalis was predominantly associated with three categories of periodontitis (60.7%). However, high-IgG antibody titer against B. gingivalis alone was found in relatively low percentage (21.4%). Most of the cases were associated with one or more of the other periodontopathic bacteria. High-IgG titer against A. actinomycetemcomitans was found in a few patients (12.5%), who showed severe and more rapid bone loss. Nine patients (16.1%) showed lower IgG antibody titer than did the healthy control subjects. Of the nine, three patients who belonged to the JP category showed the chemotaxis dysfunction of their PMNs. Some immunodepression was suspected in these patients.

Serum albumin is a specific inhibitor of apoptosis in human endothelial cells

1996 ◽  
Vol 109 (10) ◽  
pp. 2571-2580
Author(s):  
H. Zoellner ◽  
M. Hofler ◽  
R. Beckmann ◽  
P. Hufnagl ◽  
E. Vanyek ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Serum Albumin ◽  
Blood Vessels ◽  
Umbilical Vein ◽  
Specific Inhibitor ◽  
Human Albumin ◽  
Microvascular Endothelium ◽  
Bovine Albumin ◽  
Human Umbilical Vein ◽  
Endothelial Apoptosis

Excess blood vessels are removed by apoptosis of endothelial cells, however, the signals responsible for this have not been defined. Apoptosis of cultured human umbilical vein endothelial cells is induced by deprivation of serum or adhesion. In this paper, apoptosis in human umbilical vein and microvascular endothelium was induced by deprivation of serum and or adhesion. Apoptosis was confirmed on the basis of morphology, ultrastructure and internucleosomal cleavage of DNA. Loss of endothelial adhesion was found to be an early event in cultured endothelial cell apoptosis and was exploited to quantitate apoptosis. The effect of: bovine serum albumin; human serum albumin; recombinant human albumin; dithiothreitol reduced human and bovine albumin; CNBr treated human and bovine albumin as well as ovalbumin upon endothelial apoptosis was determined. Native bovine and human albumin as well as recombinant human material inhibited apoptosis at physiological concentrations with identical dose response curves in both umbilical vein and microvascular cells. Dithiothreitol treatment destroyed all protective activity while bovine but not human albumin was partially inactivated by CNBr treatment. The unrelated protein ovalbumin was not protective. Albumin did not inhibit apoptosis if cells were also deprived of adhesion. The data suggest that albumin is a specific inhibitor of human endothelial apoptosis but does not protect cells also deprived of adhesion. Reduced supply of albumin to endothelium in poorly perfused blood vessels may provide a mechanism for the removal of excess blood vessels in remodelling tissues. Also, the failure of albumin to protect endothelial cells deprived of adhesion from apoptosis may reflect the need to remove potentially micro-embolic cells detached due to trauma.

scholarly journals Large fragments of human serum albumin

1977 ◽  
Vol 161 (3) ◽  
pp. 619-625 ◽  
Author(s):  
M J Geisow ◽  
G H Beaven
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Tertiary Structure ◽  
Human Albumin ◽  
Low Ph ◽  
Bovine Albumin ◽  
Linkage Pattern ◽  
Peptic Digestion ◽  
Similar Tertiary Structure

Large fragments of human serum albumin were produced by treatment of the native protein with pepsin at pH3.5. Published sequences of human albumin [Behrens, Spiekerman & Brown (1975) Fed. Proc. Fed. Am. Soc. Exp. Biol. 34, 591; Meloun, Moravek & Kostka (1975) FEBSLett.58, 134-137]were used to locate the fragments in the primary structure. The fragments support both the sequence and proposed disulphide-linkage pattern (Behrens et al., 1975). As the pH of a solution of albumin is lowered from pH4 to pH3.5, the protein undergoes a reversible conformational change known as the N-F transition. The distribution of large fragments of human albumin digested with pepsin in the above pH region was critically dependent on pH. It appeared that this distribution was dependent on the conformation of the protein at low pH, rather than the activity of pepsin. The yields of the large fragments produced by peptic digestion at different values of pH suggested that the C-terminal region of albumin unfolds or separates from the rest of the molecule during the N-F transition. The similarity of peptic fragments of human and bovine albumin produced under identical conditions supports the proposed similar tertiary structure of these molecules.

Effect of piperacillin on morphology and viability of gram-negative bacteria

1984 ◽  
Vol 42 ◽  
pp. 218-219
Author(s):  
R. H. Liss
Keyword(s):  
Inhibitory Concentration ◽  
Cytoplasmic Membrane ◽  
Drug Binding ◽  
Gram Negative Bacteria ◽  
Bacterial Cells ◽  
Drug Induced ◽  
Penicillin Binding Proteins ◽  
Lactam Antibiotic ◽  
Drug Free ◽  
Tube Dilution

Piperacillip (PIP) is b-[D(-)-α-(4-ethy1-2,3-dioxo-l-piperzinylcar-bonylamino)-α-phenylacetamido]-penicillanate. The broad spectrum semisynthetic β-lactam antibiotic is believed to effect bactericidal activity through its affinity for penicillin-binding proteins (PBPs), enzymes on the bacterial cytoplasmic membrane that control elongation and septation during cell growth and division. The purpose of this study was to correlate penetration and binding of 14C-PIP in bacterial cells with drug-induced lethal changes assessed by microscopic, microbiologic and biochemical methods.The bacteria used were clinical isolates of Escherichia coli and Pseudomonas aeruginosa (Figure 1). Sensitivity to the drug was determined by serial tube dilution in Trypticase Soy Broth (BBL) at an inoculum of 104 organisms/ml; the minimum inhibitory concentration of piperacillin for both bacteria was 1 μg/ml. To assess drug binding to PBPs, the bacteria were incubated with 14C-PIP (5 μg/0.09 μCi/ml); controls, in drug-free medium.

Preparation of Electron Transparent Metal-Matrix Composites

1968 ◽  
Vol 26 ◽  
pp. 334-335 ◽  
Author(s):  
M. R. Pinnel ◽  
A. Lawley
Keyword(s):  
Stainless Steel ◽  
Load Transfer ◽  
Volume Fraction ◽  
Steel Wire ◽  
Initial Step ◽  
Interfacial Region ◽  
Matrix Composites ◽  
Specific Test ◽  
The Matrix ◽  
The One

Numerous phenomenological descriptions of the mechanical behavior of composite materials have been developed. There is now an urgent need to study and interpret deformation behavior, load transfer, and strain distribution, in terms of micromechanisms at the atomic level. One approach is to characterize dislocation substructure resulting from specific test conditions by the various techniques of transmission electron microscopy. The present paper describes a technique for the preparation of electron transparent composites of aluminum-stainless steel, such that examination of the matrix-fiber (wire), or interfacial region is possible. Dislocation substructures are currently under examination following tensile, compressive, and creep loading. The technique complements and extends the one other study in this area by Hancock.The composite examined was hot-pressed (argon atmosphere) 99.99% aluminum reinforced with 15% volume fraction stainless steel wire (0.006″ dia.).Foils were prepared so that the stainless steel wires run longitudinally in the plane of the specimen i.e. the electron beam is perpendicular to the axes of the wires. The initial step involves cutting slices ∼0.040″ in thickness on a diamond slitting wheel.

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