test_moissonnage_selune
type: Agent

Isolation of the receptor for the Amaranthus leucocarpus lectin from human T lymphocytes
type: Distribution
access URL: https://hal.science/hal-00085536
format: HTML
issued: 2026-05-09T23:40:20.918867
modified: 2026-05-09T23:40:20.901827

Isolation of the receptor for the Amaranthus leucocarpus lectin from human T lymphocytes
type: Dataset
contact point: Organization
  fn: CCSD
keyword: amaranthus-leucocarpus
keyword: t-cells
keyword: ontogeny
keyword: sdvbbmlife-sciences-q-biobiochemistry-molecular-biology
keyword: journal-articles
keyword: lectins
keyword: glycoproteins
keyword: infoeu-reposemanticsarticle
keyword: o-glycans
landing page: 0006-3002
description: Amaranthus leucocarpus lectin (ALL) is specific for GalNAc, and recognizes human T cells. The receptor for ALL was purified from T cells using biotin-labeled lectin and avidin-agarose as affinity matrix. It is a 70-kDa glycoprotein, constituted mainly by serine, glycine, and glutamic acid; its glycosidic portion contains mainly GalNAc; galactose, sialic acid, mannose, and GlcNAc were identified at a lower proportion. By ionic strength chromatography, as well as double dimension electrophoresis, we identified four isoforms of the ALL-receptor. N-terminal amino acid was blocked both in the ALL-receptor and its isoforms, therefore, tryptic peptides of ALL-receptor, analyzed through MALDI-TOF, were compared with the relative values obtained from the NCBInr (ProFound 2004/06/01) database. Our results indicated that the tryptic peptides obtained showed 54% homology with a DnaK-core molecular chaperone, 47% with human KIAA protein, and 44% with heat shock protein 8. The most frequent phenotype of the CD4 or CD8 ALL+ T cells was CD45RA+ CD27+; 26% of ALL+ T cells were CD25+ and 13% were CD69+, indicating that the glycoprotein recognized by ALL is present mainly on naive or quiescent T cells.
issued: 2026-05-09T23:40:20.911979
language: en
modified: 2026-05-09T23:40:20.911985