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

Modified high-affinity binding of Ni2+, Ca2+ and Zn2+ to natural mutants of human serum albumin and proalbumin.

The Biochemical journal - 1 Jul 1994

Kragh-Hansen U, Brennan S O, Minchiotti L, Galliano M

Abstract excerpt

High-affinity binding of radioactive Ni2+, Ca2+ and Zn2+ to six genetic albumin variants and to normal albumin isolated from the same heterozygote carriers was studied by equilibrium dialysis at pH 7.4. The three cations bind differently to albumin. Ni2+ binds to a site in the N-terminal region of the protein which is partially blocked by the presence of a propeptide as in proalbumin (proAlb) Varese...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites
Share to Calcium

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

Share to Genetic Variation

Share to In Vitro Techniques

Share to Kinetics

Share to Mutation

Share to Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 8037675
DOI: 10.1042/bj3010217
PMCID: PMC1137165

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

Modified high-affinity binding of Ni2+, Ca2+ and Zn2+ to natural mutants of human serum albumin and proalbumin.PMID 8037675Read ↗

High-affinity binding of laurate to naturally occurring mutants of human serum albumin and proalbumin.Semantic proximity Read ↗

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

Structure, properties, and engineering of the major zinc binding site on human albumin.Semantic proximity Read ↗

Hormone binding to natural mutants of human serum albumin.Semantic proximity Read ↗

Binding of warfarin, salicylate, and diazepam to genetic variants of human serum albumin with known mutations.Semantic proximity Read ↗

The structural characterization and bilirubin-binding properties of albumin Herborn, a [Lys240-->Glu] albumin mutant.Semantic proximity Read ↗

Structural analysis, fatty acid and thyroxine binding properties of Vancouver and Naskapi variants of human serum albumin.Semantic proximity Read ↗

High-affinity binding of warfarin, salicylate and diazepam to natural mutants of human serum albumin modified in the C-terminal end.Semantic proximity Read ↗

Structural characterization, stability and fatty acid-binding properties of two French genetic variants of human serum albumin.Semantic proximity Read ↗

In vivo and in vitro binding of fatty acids to genetic variants of human serum albumin.Semantic proximity Read ↗

Human recombinant alpha-parvalbumin and nine mutants with individually inactivated calcium- and magnesium-binding sites: biochemical and immunological properties.Semantic proximity Read ↗

Structural analysis and fatty acid-binding properties of two Croatian variants of human serum albumin.Semantic proximity Read ↗

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