Abstract
The binding of d-tubocurarine by ganglioside mixtures from chicken and bovine brain as well as by the single gangliosides GGtet1-NeuAc, GGtet2aNeuAc and GGtet3aNeuAc was demonstrated by means of equilibrium gel filtration. The sialyl-oligosaccharide derivatives of GGtet1NeuAc and GGtet2aNeuAc, however, did not bind any d-tubocurarine. A lack of binding was also found for the gangliotetraosyl-ceramide GgOse4Cer, free NeuAc, mucin and sphingomyelin. Under saturation conditions, GGtet1NeuAc bound 0.58, GGtet2aNeuAc 0.92 and GGtet3a-NeuAc 1.23 mol d-tubocurarine per mol ganglioside. Half-maximal binding was achieved between 1 and 1.5 x 10(-5)M d-tubocurarine. Ca2 was found to inhibit the binding of d-tubocurarine to gangliosides (50% at 4 x 10(-4)M Ca2). Mg2 was about 4 times less effective. Acetylcholine caused a 40% inhibition at 4 x 10(-3)M, whereas K and Na had only slight effects even at 5 x 10(-2)M.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Hoppe-Seyler´s Zeitschrift für physiologische Chemie
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
