Single amino acid substitutions of alpha 1-antitrypsin that confer enhancement in thermal stability.

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

Back to search

Article

Single amino acid substitutions of alpha 1-antitrypsin that confer enhancement in thermal stability.

The Journal of biological chemistry - 1 Apr 1994

Kwon K S, Kim J, Shin H S, Yu M H

Abstract excerpt

A recombinant alpha 1-antitrypsin variant which increased thermal stability was obtained from random mutagenesis followed by screening. The clone was identified as having a single mutation of Phe51-->Cys. Heat deactivation of purified recombinant alpha 1-antitrypsin produced in Escherichia coli r...

Topics

Amino Acid Sequence
Cloning, Molecular
Cysteine
Genetic Variation
Humans
Kinetics
Mutagenesis
Phenylalanine
Point Mutation
Polymerase Chain Reaction
Protein Denaturation
Protein Folding
Recombinant Proteins
Serpins
Thermodynamics
Urea
alpha 1-Antitrypsin

Source

Open in PubMed

Identifiers

PMID: 8144550

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8144550-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics