Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification of peanut agglutinin binding glycoproteins restricted to Hodgkin's disease-derived cell lines.

Hematological oncology - 1 Jan 2000

Flavell D J, Jones D B, Wright D H

Abstract excerpt

Peanut agglutinin (PNA) binding glycoproteins from four Hodgkin's disease (HD)-derived cell lines and a variety of cell lines/peripheral blood cells representative of the lymphoid and myeloid lineages were identified by probing nitrocellulose membranes of SDS-PAGE separated NP40 solubilized cellular glycoproteins with [125I]-labelled PNA. The two Hodgkin's cell lines Ho and L428 demonstrated the most...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Blotting, Western
Share to Cell Line
Share to SDS gene

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Glycoproteins

Share to Molecular Weight

Share to Neoplasm Proteins

Share to Phenotype

Share to Staining and Labeling

Source

Identifiers

PMID: 2468595
DOI: 10.1002/hon.2900070304

Genes

SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 10 closest

Identification of peanut agglutinin binding glycoproteins restricted to Hodgkin's disease-derived cell lines.PMID 2468595Read ↗

Recombinant glycophorins C and D as tools for studying Gerbich blood group antigens.Semantic proximity Read ↗

Antigen presenting phenotype of Hodgkin Reed-Sternberg cells: analysis of the HLA class I processing pathway and the effects of interleukin-10 on epstein-barr virus-specific cytotoxic T-cell recognition.Semantic proximity Read ↗

Differential carbohydrate binding and cell surface glycosylation of human cancer cell linesSemantic proximity Read ↗

Neutral glycosphingolipid expression in B-cell neoplasms.Semantic proximity Read ↗

Hodgkin and Reed-Sternberg cell associated monoclonal antibodies HRS-1 and HRS-2 react with activated cells of lymphoid and monocytoid origin.Semantic proximity Read ↗

Determination of HLA-A*02 antigen status in Hodgkin's disease and analysis of an HLA-A*02-restricted epitope of the Epstein-Barr virus LMP-2 protein.Semantic proximity Read ↗

Membrane glycoprotein changes associated with anthracycline resistance in HL-60 cells.Semantic proximity Read ↗

Heterogeneity of the blood group ABH antigens and variation in the expression of these antigens of secretory granules in human cervical glands. An electron microscopic observation using lectins and monoclonal antibodies.Semantic proximity Read ↗

[Glycosphingolipids of human gynecological malignant cell lines in vitro].Semantic proximity Read ↗

Lymphocyte functional antigens stabilize agglutination between Reed-Sternberg cells and T cells, but are not responsible for homotypic binding of Hodgkin's Reed-Sternberg cells.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.