Re: sulfated polyanions

[Guest guest]

here's one

http://www.fucoidan.net/modifilan.html

and modifilan is good for mercury detox.

It can't hurt me to start this right away.

got to research the others

GOT TO TAKE A NAP

i am getting obsessed as if i have to figure it all out today

[Guest guest]

Takabatake, N., Hashiba, S., Bork, S., Okamura, M., Yokoyama, N., and

Igarashi, I.: Fucoidan inhibits the in vitro growth of Babesia bovis.

J. Protozool. Res., 14: 54-60, 2004. [4]

and

http://www.pnas.org/cgi/content/full/97/15/8530

very interesting line of thought and i don't see why one only has to

use heparin. okay, stopping for now.

[Guest guest]

one more

Biol Chem, 1991 Oct 5, 266(28), 18827 - 31

Adhesion of Bordetella pertussis to sulfatides and to the GalNAc beta

4Gal sequence found in glycosphingolipids; Brennan MJ et al.; The

adherence of the human respiratory pathogen, Bordetella pertussis, to

purified glycosphingolipids was investigated using thin layer

chromatography overlay assays . Both virulent and avirulent strains

of B . pertussis bound to asialo GM1 . The bacterium did not bind to

the gangliosides GM1, GD1a, GD1b, and GT1b, nor to lactosylceramide,

trihexosylceramide, globoside, or Forssman antigen . However, after

treatment of the chromatography plates with sialidase, B . pertussis

bound to the gangliosides GM1, GM2, GD1a, GD1b, and GT1b but not to

GM3 . Comparison of the oligosaccharide structures of these

gangliosides suggests that the minimum sugar structure needed for

avid bacterial binding is GalNAc beta 4Gal . This structure has been

previously implicated as a receptor for other human respiratory

pathogens (Krivan, H . C., , D . D., Ginsburg, V . (1988)

Proc . Natl . Acad . Sci . U.S.A 85, 6157-6161) . Virulent strains of

B . pertussis also bound specifically to sulfatide . This response

was dose-dependent and inhibited by the anionic polysaccharide

dextran sulfate . The sulfated-sugars dextran sulfate, fucoidan, and

heparin inhibited the attachment of virulent strains of B . pertussis

to human WiDr cells and to hamster trachea cells indicating that

sulfatides on the surface of mammalian cells may function as a

receptor for B . pertussis . The occurrence of both sulfatides and

asialo GM1 in human lung and trachea suggests that these glycolipids

may serve as specific receptors for B . pertussis.