Quantitive estimation of sialic acids

Svennerholm, Lars

doi:10.1016/0006-3002(57)90254-8

Cited by 2,660 publications

(395 citation statements)

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“…The resorcinol reagent spray [12] was used to locate the gangliosides which were identified by running markers in parallel. The relative distribution was calculated from profiles obtained by reflective densitometry using a Vernon densitometer ( fig.…”

Section: Gxmentioning

confidence: 99%

Gangliosides of whole retina and rod outer segments

et al. 1973

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Section: Gxmentioning

confidence: 99%

Gangliosides of whole retina and rod outer segments

et al. 1973

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“…Gangliosides which bind best to TSH in vitro, i.e., (7,9), the subunit believed to be associated with adenylate cyclase activation (5,6 Gangliosides GM3, GM2, GM1, GD1a, GD1b, and GT1 were obtained as previously described (1,15,16). Each ganglioside used in these experiments was at least 99% pure following rechromatography, visualization with resorcinol reagent, and densitometric analysis (16); gangliosides were quantitated from their sialic acid content using a micro-modification of the resorcinol method of Svennerholm (17).…”

mentioning

confidence: 99%

Cholera toxin interactions with thyrotropin receptors on thyroid plasma membranes.

Mullin¹,

Aloj²,

Fishman³

et al. 1976

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

115

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Unlabeled cholera toxin inhibits [125I] Cholera toxin can stimulate adenylate cyclase activity in thyroid plasma membranes. Its effect is not additive with that of thyrotropin, and cholera toxin can inhibit thyrotropin stimulation of the adenylate cyclase activity. NAD enhances cholera toxin stimulation of adenylate cyclase activity but has no enhancing effect on the stimulatory activity exhibited by thyrotropin.The GM1 ganglioside [galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl)galactosylglucosylceramideI in thyroid plasma membranes can be tritiated by treating membranes with galactose oxidase, followed by reduction with 3-H-labeled sodium borohydride. Cholera toxin at a concentration which yields maximal inhibition of thyrotropin binding to thyroid plasma membrane receptors prevents the labeling of GMI.Fluorescence data indicate that the interaction between cholera toxin and GM1 results in a conformational change in the cholera toxin molecule. Analogous conformational alterations cannot be detected upon exposure of cholera toxin to 5-fold higherIn a previous report (1) we suggested that thyrotropin (TSH) and cholera toxin have an analogous mode of interaction with receptors on thyroid plasma membranes. We hypothesized that in both the case of TSH and cholera toxin, the ,B or B subunit interacts with specific cell surface receptors having gangliosides or ganglioside-like oligosaccharides as part of their core structures. This binding induces a conformational change in the hormone or toxin which results in translocation of an "active" a or A subunit within the cell membrane and adenylate cyclase activation. The evidence which led to this hypothesis can be summarized as follows. Thyrotropin and cholera toxin both bindAbbreviations:

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“…Total lipid was determined gravimetrically and lipid phosphorus by colorimetric assay [21 ]. Gangliosides were separated by thin-layer chromatography on 500/zm layers of Silica gel G developed in chloroform-methanol-28% ammonia-water (60:30:7:3, by volume) and the ganglioside bands were detected with resorcinol reagent [22].…”

Section: Methodsmentioning

confidence: 99%