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

The effect of the Z mutation on the ability of alpha 1-antitrypsin to prevent neutrophil mediated tissue damage.

Biochimica et biophysica acta - 29 Nov 1994

Llewellyn-Jones C G, Lomas D A, Carrell R W, Stockley R A

Abstract excerpt

Recent studies have shown that alpha 1-antitrypsin (alpha 1-AT) from Z antitrypsin deficiency subjects has a slightly lower association rate constant with neutrophil elastase (NE) than alpha 1-AT from normal subjects, although it is unknown whether this is of clinical importance. We have purified alpha 1-AT from a normal (M alpha 1-AT) and from a deficient (Z alpha 1-AT) subject and have confirmed that the...

Read the complete abstract on PubMed

Topics

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

Share to alpha 1-Antitrypsin
Share to Connective Tissue
Share to Fibronectins

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

Share to Homozygote

Share to Mutation

Share to Neutrophils

Share to Pancreatic Elastase

Share to Phenotype

Source

Identifiers

PMID: 7986822
DOI: 10.1016/0925-4439(94)90089-2

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

The effect of the Z mutation on the ability of alpha 1-antitrypsin to prevent neutrophil mediated tissue damage.PMID 7986822Read ↗

Kinetic characterisation of alpha-1-antitrypsin F as an inhibitor of human neutrophil elastase.Semantic proximity Read ↗

Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin.Semantic proximity Read ↗

Why has it been so difficult to prove the efficacy of alpha-1-antitrypsin replacement therapy? Insights from the study of disease pathogenesis.Semantic proximity Read ↗

Function of a rare variant of alpha-1-antitrypsin, phenotype P(i) EFranklin S, a poor inhibitor of human neutrophil elastase.Semantic proximity Read ↗

A protein structural approach to the solution of biological problems: alpha 1-antitrypsin as a recent example.Semantic proximity Read ↗

Alpha-1 Antitrypsin-Deficient Macrophages Have Increased Matriptase-Mediated Proteolytic Activity.Semantic proximity Read ↗

The Z type variation of human alpha 1-antitrypsin causes a protein folding defect.Semantic proximity Read ↗

The multiple facets of alpha-1-antitrypsin.Semantic proximity Read ↗

The mechanism of Z alpha 1-antitrypsin accumulation in the liver.Semantic proximity Read ↗

Alpha-1-antitrypsin PLowell: a normally functioning variant present in low concentration.Semantic proximity Read ↗

Inhibition of intracellular degradation increases secretion of a mutant form of alpha1-antitrypsin associated with profound deficiency.Semantic proximity Read ↗

Protein Z.Semantic proximity Read ↗

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