Albumin Redhill (-1 Arg, 320 Ala----Thr): a glycoprotein variant of human serum albumin whose precursor has an aberrant signal peptidase cleavage site.

doi:10.1073/pnas.87.1.26

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Article

Albumin Redhill (-1 Arg, 320 Ala----Thr): a glycoprotein variant of human serum albumin whose precursor has an aberrant signal peptidase cleavage site.

Proceedings of the National Academy of Sciences of the United States of America - 1 Jan 1990

Brennan S O, Myles T, Peach R J, Donaldson D, George P M

Abstract excerpt

Albumin Redhill is an electrophoretically slow genetic variant of human serum albumin that does not bind 63Ni2+ and has a molecular mass 2.5 kDa higher than normal albumin. Its inability to bind Ni2+ was explained by the finding of an additional residue of Arg at position -1. This did not explain...

Topics

Alanine
Amino Acid Sequence
Arginine
Base Sequence
Endopeptidases
Genes
Genetic Variation
Humans
Membrane Proteins
Molecular Sequence Data
Oligonucleotide Probes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Peptide Fragments

Peptide Mapping

Polymerase Chain Reaction

Prealbumin

Sequence Homology, Nucleic Acid

Serine Endopeptidases

Serum Albumin

Source

Open in PubMed Open full text

Identifiers

PMID: 2104980
DOI: 10.1073/pnas.87.1.26
PMCID: PMC53192

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2104980-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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