Free thiol groups and labile disulfide bonds in the IgG fraction of human serum

Schauenstein, E.; Sorger, S.; Reiter, Monika; Dachs, F.

doi:10.1016/0022-1759(82)90303-9

Cited by 27 publications

(26 citation statements)

References 6 publications

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“…However, free sulfhydryls has been routinely detected in IgG molecules, including IgG from serum and recombinant mAbs ( Table 1). [28][29][30][31][32][33][34][35] It is worthwhile to discuss two important observations in Table 1. First, higher level of free sulfhydryls was detected under denaturing conditions compared with native conwhile the two major non-classical structures were referred to as IgG 2 B and IgG 2 -A/B, the latter being considered a structural intermediate between IgG 2 A and IgG 2 B (Fig.…”

Section: Free Sulfhydrylsmentioning

confidence: 99%

Disulfide bond structures of IgG molecules

Liu

May

2012

mAbs

377

204

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Section: Free Sulfhydrylsmentioning

confidence: 99%

Disulfide bond structures of IgG molecules

Liu

May

2012

mAbs

377

204

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“…This indicated an additional binding of 35S-NBSSBN (or its half molecules) to proteins belonging to this serum component. As immunoglobulins G, making up to 70-75% of '/-globulins, had been presumably involved, monomeric IgG was isolated in Tris-HCl-buffer pH 7.2 from serum [7,8] and mixed with a solution of unlabelled NBSSBN. After 30 minutes, a yellow eolour appeared with absorption maximum at 410 nm.…”

Section: Detection Of Free Sulfhydril Groups (Sh) and (Ss)* In Human Igomentioning

confidence: 99%

Reactive disulfide bonds in immunoglobulin G. A unique feature in serum proteins of different species

Schauenstein

Dachs

et al. 1996

IUBMB Life

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A reactive disulfide bond (SS)* was detected and characterized in IgG of humans, rats and mice by virtue of disulfide interchange with dithionitrobenzoate. (SS)* was found exclusively in human IgG1 and rat IgG2b. In human IgG1 (SS)* was identified as the upper one of the two interheavy bridges in the hinge, where it appears to take part in complement activation. The biological significance of (SS)* in IgG was underlined by the fact that no other serum proteins were found to exhibit a similar reactivity.

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“…Using dithionitrobenzoate (DTNB) as a sulfhydryl reagent, we have found [1,2] that human IgG con tained an average of 0.24±0.02 free SH groups/mol. Prolonged treatment (24 h) of serum with this reagent resulted in the liberation of a total (ZS) of 1.51 ±0.39 thioanions from the isolated and reduced IgG frac tion.…”

Section: Introductionmentioning

confidence: 99%

Labile Disulfide Bonds and Free Thiol Groups in Human IgG I.

Schauenstein

Dachs²,

Reiter

et al. 1986

Int Arch Allergy Immunol

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The content of free SH groups (about 0.24) and labile S-S bonds (about 0.64) per mole human IgG can be differentially determined by the reaction with 5,5′-dithio(2,2′-dinitro)benzoate (DTNB) for 30 min and 24 h, respectively. Highly significant linear correlations were found between the number of labile S-S and the percentage of IgG₁, and the number of free SH and the percentage of IgG₂ of the total IgG fraction. It is concluded that the IgG₁ molecule contains one S-S bond which is opened during the 24 h interaction with DTNB by a disulfide exchange reaction. This was also confirmed by the investigation of pure monomeric IgG₁. The splitting of this bond does not alter molecular weight, antigenic properties or antigen binding activity, but reduces significantly the complement binding activity of IgG. On the other hand, one free SH group could be found in the IgG₂ molecule. Changes have been observed in SH and S-S levels of total IgG in patients with various malignant diseases that are to be explained by corresponding changes of the percentages of IgG₁ and IgG₂.

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Free thiol groups and labile disulfide bonds in the IgG fraction of human serum

Cited by 27 publications

References 6 publications

Disulfide bond structures of IgG molecules

Disulfide bond structures of IgG molecules

Reactive disulfide bonds in immunoglobulin G. A unique feature in serum proteins of different species

Labile Disulfide Bonds and Free Thiol Groups in Human IgG I.

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