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

Production of recombinant human alpha1-microglobulin and mutant forms involved in chromophore formation.

Protein expression and purification - 1 May 2007

Kwasek Anna, Osmark Peter, Allhorn Maria, Lindqvist Annika, Akerström Bo, Wasylewski Zygmunt

Abstract excerpt

Alpha(1)-Microglobulin, a 26 kDa lipocalin present in plasma and tissues, carries a set of unknown chromophores, bound to C34, K92, K118 and K130, which cause its charge and size heterogeneity. In man, the protein is found in two forms, full length and lacking the C-terminal tetrapeptide LIPR (t-alpha(1)-microglobulin), both which are heme-binding and the latter with heme-degrading properties. We report cloning...

Read the complete abstract on PubMed

Topics

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

Share to Alpha-Globulins
Share to Chromatography, Affinity

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

Share to Chromatography, Gel

Share to Inclusion Bodies

Share to Isoelectric Focusing

Share to Radioimmunoassay

Share to Serum Albumin, Bovine

Share to Spectrophotometry, Ultraviolet

Source

Identifiers

PMID: 17169572
DOI: 10.1016/j.pep.2006.10.023

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 · 12 closest

Production of recombinant human alpha1-microglobulin and mutant forms involved in chromophore formation.PMID 17169572Read ↗

Structural and biochemical characterization of two heme binding sites on α1-microglobulin using site directed mutagenesis and molecular simulation.Semantic proximity Read ↗

Redox properties of the lipocalin alpha1-microglobulin: reduction of cytochrome c, hemoglobin, and free iron.Semantic proximity Read ↗

Structure, Functions, and Physiological Roles of the Lipocalin α1-Microglobulin (A1M)Semantic proximity Read ↗

Anticalin® proteins: from bench to bedsideSemantic proximity Read ↗

The single mutation Phe173 --> Ala induces a molten globule-like state in murine interleukin-6.Semantic proximity Read ↗

Replacement of tyr62 by trp in the designer protein milk bundle-1 results in significant improvement of conformational stability.Semantic proximity Read ↗

Characterization of the l-ferritin variant 460InsA responsible of a hereditary ferritinopathy disorder.Semantic proximity Read ↗

Disposal of iron by a mutant form of lipocalin 2.Semantic proximity Read ↗

A rapid microbore HPLC method for determination of primary structure of beta-lactoglobulin genetic variants.Semantic proximity Read ↗

Production of a 135-residue long N-truncated human keratinocyte growth factor 1 in Escherichia coliSemantic proximity Read ↗

Structure, stability and biological properties of a N-terminally truncated form of recombinant human interleukin-6 containing a single disulfide bond.Semantic proximity Read ↗

Lactoferrin: structure, function and applicationsSemantic proximity Read ↗

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