Molecular basis of human band-3 mutation associated with increased anion transport.

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

Back to search

Article

Molecular basis of human band-3 mutation associated with increased anion transport.

Experimental and clinical immunogenetics - 1 Jan 1994

Kay M M, Bosman G, Johnson R C, Poulin J, Lawrence C, Goodman J

Abstract excerpt

Band 3, the anion transporter, is a ubiquitous protein. It is present in brain and all other tissues. Not only is band 3 present in cell membranes, but also in nuclear, Golgi, and mitochondrion membranes. Band 3 is involved in respiration, acid-base balance, and is the major structural protein li...

Topics

Anion Exchange Protein 1, Erythrocyte
Anions
Ankyrins
Blood Glucose
Creatinine
Cytochalasin B
Female
Glyceraldehyde-3-Phosphate Dehydrogenases
Humans
Immunoglobulin G
Ion Transport
Male
Mutation
Peptide Fragments
Structure-Activity Relationship

Source

Open in PubMed

Identifiers

PMID: 7857667

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7857667-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics