Purification of bovine serum paraoxonase and its immobilization on Eupergit C 250 L by covalent attachment

2014 ◽  
Vol 30 (1) ◽  
pp. 69-74
Author(s):  
Murat Sayın ◽  
Ozen Ozensoy Guler
Keyword(s):  
Bovine Serum ◽  
Covalent Attachment ◽  
Eupergit C ◽  
Serum Paraoxonase

Application of Colloidal Palladium Nanoparticles for Labeling in Electron Microscopy

2011 ◽  
Vol 17 (5) ◽  
pp. 810-816 ◽  
Author(s):  
Marie Vancová ◽  
Miroslav Šlouf ◽  
Jan Langhans ◽  
Eva Pavlová ◽  
Jana Nebesářová
Keyword(s):  
Electron Microscopy ◽  
Bovine Serum ◽  
Palladium Nanoparticles ◽  
Secretory Granules ◽  
Protein A ◽  
Pd Nanoparticles ◽  
Single Step ◽  
Covalent Attachment ◽  
Equivalent Diameter ◽  
Functional Protein

AbstractThe application of palladium nanoparticles as electron-dense markers for labeling in both transmission and scanning electron microscopy requires their conjugation to a specific protein. The conjugation protocol described here includes the dihydrolipoic acid (DHLA) capping of Pd nanoparticles (8 nm equivalent diameter) and their subsequent covalent attachment to functional protein molecules such as streptavidin, protein A, or avidin. The single-step reaction was mediated using the cross-linking agent ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC). The final Pd conjugates were fully functional, as demonstrated by labeling of ultrathin resin sections of either bovine serum albumin or secretory granules of the salivary gland isolated from the partially fed female Ixodes ricinus tick. The results of bovine serum labeling were quantified, statistically evaluated, and compared with results obtained using commercially available gold particle conjugates (10 nm diameter). The highest values of labeling density were achieved using both streptavidin-Pd (106 ± 7 particles/μm2) and protein A-Au conjugates (130 ± 18 particles/μm2) compared to a commercial streptavidin-Au (66 ± 16 particles/μm2) and protein A-Pd conjugates (70 ± 11 particles/μm2). The concentrations of both DHLA and EDC, pH during conjugation, and finally thorough washing away of unbound proteins crucially influenced conjugation.

Antibody to an artificial disaccharide antigen cross-reactive with Neisseria gonorrhoeae lipopolysaccharide

1979 ◽  
Vol 57 (5) ◽  
pp. 367-371 ◽  
Author(s):  
David R. Bundle
Keyword(s):  
Cell Wall ◽  
Bovine Serum Albumin ◽  
Neisseria Gonorrhoeae ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Covalent Attachment ◽  
Passive Hemagglutination ◽  
Streptococcus Faecalis ◽  
Artificial Antigen

An artificial antigen was prepared from 4-O-β-D-galactopyranosyl-D-glucose (lactose) and 8-ethoxycarbonyloctanol. Covalent attachment to bovine serum albumin provided an antigen that elicited antilactose antibody in rabbits and goat. These antibodies were active against Neisseria gonorrhoeae lipopolysaccharide in passive hemagglutination tests. The same antibody agglutinated cells of Streptococcus faecalis, strain N, and precipitated the lactose-containing cell wall diheteroglycan of this organism. Fractionation of rabbit and goat antibody raised against the synthetic antigen of S. faecalis vaccine provided two antibody fractions only one of which, eluted from the immunoadsorbent by galactose, was active against N. gonorrhoeae lipopolysaccharide.

Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid

2002 ◽  
Vol 78 (4) ◽  
pp. 443-455 ◽  
Author(s):  
Harshadrai M Rawel ◽  
Sascha Rohn ◽  
Hans-Peter Kruse ◽  
Jürgen Kroll
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Chlorogenic Acid ◽  
Bovine Serum ◽  
Structural Changes ◽  
Covalent Attachment

In vitro efficacy of some cattle drugs on bovine serum paraoxonase 1 (PON1) activity

2011 ◽  
Vol 27 (5) ◽  
pp. 722-729 ◽  
Author(s):  
Mikail Arslan ◽  
Nahit Gencer ◽  
Oktay Arslan ◽  
Ozen Ozensoy Guler
Keyword(s):  
Bovine Serum ◽  
Paraoxonase 1 ◽  
Pon1 Activity ◽  
Serum Paraoxonase

Localization of Intracellular Antigens in thin Sections with Ferritin Labeled Antibody

1970 ◽  
Vol 28 ◽  
pp. 174-175
Author(s):  
M.S. Shahrabadi ◽  
T. Yamamoto
Keyword(s):  
Bovine Serum Albumin ◽  
Bovine Serum ◽  
Antigenic Determinants ◽  
Conjugate Prior ◽  
Thin Sections ◽  
Specific Attachment ◽  
Intracellular Antigen ◽  
Antigen Antibody ◽  
Ideal Method ◽  
The Ideal

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.

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.

Albumin-Induced Endocytic Vacuoles in Tetrahymena Pyrijormis

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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