Search PubMed⌕ Search
Home/Archive/PubMed

PubMed · 559421

A rapid, quantitative, and highly specific assay for carbohydrate-binding proteins.

J Howard·L Shannon
View original source ↗Export metadata ↓

Abstract

The source did not provide an abstract. Follow the original record for more information.

Explore related subjects

AcetylgalactosamineAnimalsAntibodiesBinding Sites, AntibodyLectinsPlant ExtractsPlant LectinsRabbitsSepharoseGlycine maxJournal ArticleResearch Support, U.S. Gov't, Non-P.H.S.

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

J Howard, L Shannon. 1977-05-01. A rapid, quantitative, and highly specific assay for carbohydrate-binding proteins.. https://doi.org/10.1016/0003-2697(77)90398-0

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1979

Gangliosides of human erythrocytes. A novel ganglioside with a unique N-acetylneuraminosyl-(2 leads to 3)-N-acetylgalactosamine structure.

A novel ganglioside having both N-acetylgalactosamine and N-acetylglucosamine was isolated from human erythrocyte membranes. Its structure was characterized by successive exoglycosidase treatment, methylation analysis, and direct-probe mass spectrometry of permethylated intact and desialylated glycolipid. The core structure of the ganglioside was found to be N-acetylgalactosaminyl paragloboside with sialosyl substitution by 2 leads to 3 linkage at the terminal GalNAc residue: NeuNAc alpha 2 leads to 3 GalNAc beta 1 leads to -3Gal beta 1 leads to 4 GlcNAc beta 1 leads to 3 Gal beta 1 leads to 4Glc leads to Cer. The ganglioside was characterized by the presence of a ceramide with myristic acid as the major component.

Acetylgalactosamine↗