The preparation of latex particles with covalently bound polyamines, IgG and measles agglutinins and their use in visual agglutination tests

Quash, G.; Roch, Anne-Marie; Niveleau, Alain; Grange, J.; Keolouangkhot, T.; Huppert, J.

doi:10.1016/0022-1759(78)90069-8

Cited by 87 publications

(30 citation statements)

References 12 publications

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“…[23][24][25] For the preparation carboxylated particles with a diameter of 2.0 mm (Polysciences Europe, Eppelheim, Germany) were used. The beads from a 50 ml bead suspension (26.5 mg/ml) were washed twice with 200 ml of carbonate buffer (100 mM sodium carbonate, 100 mM sodium bicarbonate (pH 9.6)) and three times with 200 ml buffer A (20 mM phosphate buffer (pH 4.5)).…”

Section: Preparation Of Anti-digoxigenin Antibodies Covered Beadsmentioning

confidence: 99%

Binding of TmHU to Single dsDNA as Observed by Optical Tweezers

Salomo

Kroy²,

Kegler

et al. 2006

Journal of Molecular Biology

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Section: Preparation Of Anti-digoxigenin Antibodies Covered Beadsmentioning

confidence: 99%

Binding of TmHU to Single dsDNA as Observed by Optical Tweezers

Salomo

Kroy²,

Kegler

et al. 2006

Journal of Molecular Biology

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“…Chemical or enzymic oxidation of antibody oligosaccharides to aldehydes yields unique functional groups on the molecule, which can selectively react with compounds containing, for example, amines, hydrazines, hydrazides, and semicarbazides (41)(42)(43). Since the sites of attachment of oligosaccharides to antibodies are specific and distal to the antibody-combining site (29), selective coupling to aldehydes should yield more uniform antibody conjugates with unimpaired antigen-binding characteristics.…”

Section: Discussionmentioning

confidence: 99%

Site-specific covalent modification of monoclonal antibodies: in vitro and in vivo evaluations.

Rodwell¹,

Alvarez²,

Lee³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

212

101

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drugs (9, 26-28) in attempts to target these agents to tumors. These latter modifications all involve covalent attachment to tyrosines, e-amino side chains of lysines, carboxyl side chains of aspartic and glutamic acids, or sulfhydryl groups generated by reduction of cystines. Although each of these applications has shown promise, none, as yet, has reached the point of proven clinical utility. Since so many of the diagnostic and therapeutic applications envisioned for monoclonal antibodies require coupling of antibodies to other substances, there is a need for methods of covalent modification that can be used on a broad spectrum of different antibodies with minimal effect on antigen binding properties. This paper will present a strategy for site-specific covalent modification of antibodies based upon attachment through the oligosaccharide moiety of the molecule. Because of the restricted localization of the glycosylation sites on immunoglobulins, such an approach offers the potential advantage of modification of the antibodies at a site distal to the antigen combining site (29). Data will be presented that first compares the effect of various techniques of monoclonal antibody modification on the antigenbinding homogeneity and affinity of the conjugate. Second, the comparative in vivo biodistribution and tumor localization of additional radiolabeled monoclonal antibodies will be presented using nude mice bearing subcutaneous tumor xenografts. MATERIALS AND METHODSIn Vitro Binding. The mouse monoclonal anti-phosphocholine IgM, HPCM2 (30), was grown in BALB/c mice and purified from ascites by ammonium sulfate precipitation, followed by affinity chromatography (31). The following conjugates of HPCM2 were prepared.(i) For oligosaccharide attachments, the oligosaccharides moieties were oxidized to aldehydes by incubation in the dark with 10-30 mM NaIO4 in phosphate-buffered saline (0.15 M NaCl/0.01 M sodium phosphate) at pH 6.0 on ice for 1 hr. After passage through a Sephadex G-25 column equilibrated with phosphate-buffered saline at pH 6.0, oxidized antibody was incubated with a 270-fold molar excess of 1,6-diaminohexylethylenediaminedi-o-hydroxyphenylacetic acid (1,6-diaminohexyl-EDDHA) § for 1 hr at room temperature. Sodium cyanoborohydride (Aldrich) was added to a final concentration of 10 mM, and the solution was incubated for an additional 4 hr and then dialyzed at 4°C versus several changes of phosphate-buffered saline.(ii) For aspartic/glutamic acid attachments, the antibody was incubated in 20 mM 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (Sigma) at pH 5.9 for 2 hr at room temperature. The 1,6-diaminohexyl-EDDHA was added to a final concentration of 10 mM, and the solution was incubated at room temperature for an additional 2 hr. Ten microliters of 1 M ethanolamine was added, and, after 1 hr the reaction mixture was dialyzed versus phosphate-buffered saline.(iii) For lysine attachments, the scheme for aspartic/glutamic acid modification was used except that EDDHA (5 mM; Sigma) replaced the 1,6-diamino...

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“…In the former experiment, the concentration of periodate and oxidation time used were based on literature values for oxidizing glycoproteins such as IgG [22]. We therefore decided to examine the influence of these 2 parameters on the kinetics of HCMV inactivation.…”

Section: The Effect Of Periodate Oxidation On Hcmv Infectivity In Vitromentioning

confidence: 99%

Inactivation of human cytomegalovirus by sodium periodate oxidation

Geoffroy

Ogier

Chantepie

et al. 1994

Archives of Virology

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Human cytomegalovirus (HCMV), oxidized by sodium periodate (NaIO4), is incapable of giving rise to viral progeny in cell culture. At a NaIO4 concentration as low as 5 mM, there is a loss of at least 6 logs of viral infectivity which occurs very rapidly (less than 5 min). Further, the inactivation is a first-order reaction depending on the periodate concentration. Adsorption to the cell surface, penetration into cells, and penetration of the viral DNA into cell nuclei were found to occur identically in mock oxidized and oxidized HCMV. Since the carbohydrate moiety of viral glycoproteins was the target of periodate attack, these observations strongly suggest that the structural integrity of the sugar residues is not a prerequisite for adsorption and penetration. Nevertheless, no evidence for viral DNA or protein synthesis was detected in cells infected with oxidized virus, and even after 3 weeks in culture, no cytopathic effect was observed.

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The preparation of latex particles with covalently bound polyamines, IgG and measles agglutinins and their use in visual agglutination tests

Cited by 87 publications

References 12 publications

Binding of TmHU to Single dsDNA as Observed by Optical Tweezers

Binding of TmHU to Single dsDNA as Observed by Optical Tweezers

Site-specific covalent modification of monoclonal antibodies: in vitro and in vivo evaluations.

Inactivation of human cytomegalovirus by sodium periodate oxidation

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