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

Pharmacokinetics of extracellular-superoxide dismutase in the vascular system.

Free radical biology & medicine - 1 Feb 1993

Karlsson K, Sandström J, Edlund A, Edlund T, Marklund S L

Abstract excerpt

Extracellular-superoxide dismutase C (EC-SOD C) is a secretory tetrameric Cu- and Zn-containing glycoprotein which has high affinity for heparin and heparan sulfate. Upon intravenous injection into rabbits, recombinant human (rh) EC-SOD C was found to be rapidly 97-98% sequestered to the vascular wall, forming an equilibrium with the plasma phase. Recombinant EC-SOD truncation variants with reduced, T216, and...

Read the complete abstract on PubMed

Topics

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

Share to Free Radicals
Share to Genetic Variation
Share to Heparin

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

Share to Kidney

Share to Kinetics

Share to Rabbits

Share to Recombinant Proteins

Share to Superoxide Dismutase

Source

Identifiers

PMID: 8381106
DOI: 10.1016/0891-5849(93)90009-j

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.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Pharmacokinetics of extracellular-superoxide dismutase in the vascular system.PMID 8381106Read ↗

A site-directed mutant of Cu,Zn-superoxide dismutase modeled after native extracellular superoxide dismutase.Semantic proximity Read ↗

10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain.Semantic proximity Read ↗

Protective role of extracellular superoxide dismutase in hemodialysis patients.Semantic proximity Read ↗

Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface.Semantic proximity Read ↗

An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases.Semantic proximity Read ↗

Vascular effects of the human extracellular superoxide dismutase R213G variant.Semantic proximity Read ↗

Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase.Semantic proximity Read ↗

A common polymorphism in extracellular superoxide dismutase affects cardiopulmonary disease risk by altering protein distribution.Semantic proximity Read ↗

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