Some observations on the periodate oxidation of amino compounds

Clamp, J. R.; Hough, L.

doi:10.1042/bj1010120

Cited by 23 publications

(15 citation statements)

References 5 publications

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“…This oxidation of sulfhydryl groups to sulfoxides could be expected to cause conformational changes which would deactivate the toxin as similarly speculated for alkylation. Another possibility arises; since periodate oxidation is not as specific for sulfhydryl groups as IA alkylation, the deactivation could be attributed to oxidation of other amino acids or even a carbohydrate moiety if one exists (5,6).…”

Section: Discussionmentioning

confidence: 99%

Streptolysin O II. Relationship of Sulfyhdryl Groups to Activity

Epps

Andersen

1971

Infect Immun

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Streptolysin O (SO), a group A streptococcal toxin, exists in two forms, a reduced active state and an oxidized reversibly inactive state. Activity is measured by red blood cell hemolysis. SO is a labile toxin, and, with time, activity is irreversibly lost. The rate of activity loss is slowed by incubation with 0.1 m 2-mercaptoethanol or 0.01 m ethylenediaminetetraacetic acid (EDTA). The effect of EDTA can be reversed by excess MgSO 4 . Reversibly oxidized SO is activated by cleavage of disulfide bonds. When the free sulfhydryl groups of the active SO are alkylated with iodoacetamide, complete and irreversible loss of activity results. Periodate (0.01 m ) oxidation also causes complete loss of activity which may be due to oxidation of sulfhydryl groups. SO in the active form reacts with Fe 2+ , Cu 2+ , Ca 2+ , and Mg 2+ , causing loss of activity in various degrees depending on the ions and the concentration used. Ferric and cupric ions are most effective and cause loss of activity at concentrations on the order of 10 −4 m . The reversibly oxidized form of SO is not influenced by exposure to cupric ions (0.01 m ), indicating that the reaction is only with the active form of SO, probably involving the free sulfhydryl groups. These groups may be responsible for the direct binding of the toxin to the target membrane or for the maintenance of the proper conformation for activity.

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Section: Discussionmentioning

confidence: 99%

Streptolysin O II. Relationship of Sulfyhdryl Groups to Activity

Epps

Andersen

1971

Infect Immun

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“…Under the conditions used complete cleavage of the theoretically susceptible bonds occurs within 5 min, but a slower secondary reaction also takes place, resulting in the loss of the a-NH2 group as judged by its non-adsorption on a sulphonic acid ion-exchange resin. In a study of the reaction of amino compounds with periodate, Clamp & Hough (1966) found that oxidation of amino acids occurs according to the general equation:…”

Section: Proportion Of Keto Form Of Cross-links In Various Collagensmentioning

confidence: 99%

The chemistry of the collagen cross-links. The mechanism of stabilization of the reducible intermediate cross-links

Robins

Bailey

1975

Biochemical Journal

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The periodate-degradation technique was used to demonstrate the mechanism by which the reducible cross-links of collagen are stabilized. In all the tissues examined, Smith degradations of the 3H-labelled cross-links indicated that dihydroxylysinonorleucine is derived solely from hydroxylysino-5-oxonorleucine, the Amadori-rearranged product of the original condensation reaction. Monohydroxylysinonorleucine exists in both keto and aldimine forms, the former being derived from hydroxyallysine and the latter from allysine. Their relative proportions are tissue-dependent and are related to the degree of hydroxylation of the specific lysine residues in both the telopeptides and the triple helix.

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“…These, of course, are seriously limiting factors, as the former can adversely affect the immunoreactivity of the antibody, and the latter can defeat the purpose of the site-selective modification strategy entirely. 13 …”

Section: Introductionmentioning

confidence: 99%

Enzyme-Mediated Methodology for the Site-Specific Radiolabeling of Antibodies Based on Catalyst-Free Click Chemistry

et al. 2013

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An enzyme- and click chemistry-mediated methodology for the site-selective radiolabeling of antibodies on the heavy chain glycans has been developed and validated. To this end, a model system based on the prostate specific membrane antigen-targeting antibody J591, the positron-emitting radiometal 89Zr, and the chelator desferrioxamine has been employed. The methodology consists of four steps: (1) the removal of sugars on the heavy chain region of the antibody to expose terminal N-acetylglucosamine residues; (2) the incorporation of azide-modified N-acetylgalactosamine monosaccharides into the glycans of the antibody; (3) the catalyst-free click conjugation of desferrioxamine-modified dibenzocyclooctynes to the azide-bearing sugars; and (4) the radiolabeling of the chelator-modified antibody with 89Zr. The site-selective labeling methodology has proven facile, reproducible, and robust, producing 89Zr-labeled radioimmunoconjguates that display high stability and immunoreactivity in vitro (>95%) in addition to high selective tumor uptake (67.5 ± 5.0 %ID/g) and tumor-to-background contrast in athymic nude mice bearing PSMA-expressing subcutaneous LNCaP xenografts. Ultimately, this strategy could play a critical role in the development of novel well-defined and highly immunoreactive radioimmunoconjugates for both the laboratory and clinic.

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Some observations on the periodate oxidation of amino compounds

Cited by 23 publications

References 5 publications

Streptolysin O II. Relationship of Sulfyhdryl Groups to Activity

Streptolysin O II. Relationship of Sulfyhdryl Groups to Activity

The chemistry of the collagen cross-links. The mechanism of stabilization of the reducible intermediate cross-links

Enzyme-Mediated Methodology for the Site-Specific Radiolabeling of Antibodies Based on Catalyst-Free Click Chemistry

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