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Determination of the role of cuticular carbohydrates in the hemocompatibility of Dirofilaria immitis (Nematoda).
J Biomed Mater Res
February 1993
Department of Bioengineering, Clemson University, South Carolina.
We have partially characterized surface glycoproteins of the canine heartworm, Dirofilaria immitis. Histochemical studies indicated the presence of neutral and acidic mucopolysaccharides at the blood-cuticle interface. Fluorescein isothiocyanate-conjugated lectin binding patterns suggested the presence of alpha-D-glucosyl and/or alpha-D-mannosyl, beta-galactosyl, N-acetylneuraminyl and N-acetylated-D-hexosaminyl (sialic and glucuronic acids, respectively) terminal residues among the constituent sugars of the glycocalyx.
View Article and Find Full Text PDFAscaris suum: stage-specific differences in lectin binding to the larval cuticle.
Exp Parasitol
October 1991
U.S. Department of Agriculture, Agricultural Research Service, Beltsville, Maryland 20705.
A glycosylated component with affinity for wheat germ agglutinin (specific binding to n-acetyl-D-glucosamine monomers and oligomers) and weak affinity for poke weed mitogen (specific binding to n-acetyl-D-glucosamine oligomers) was detected temporally on the surface of Ascaris suum larvae developing in vitro and on in vivo-derived larvae. The component was identified on the surface of in vitro-derived late second stage larvae, on all late third stage larvae (derived from pig lung), and all fourth stage larvae (obtained from pig intestines and from in vitro culture) of A. suum.
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