Evidence for difference in the roles of two cysteine residues involved in disulfide bond formation in the folding of human lysozyme.

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Article

Evidence for difference in the roles of two cysteine residues involved in disulfide bond formation in the folding of human lysozyme.

The Journal of biological chemistry - 5 May 1990

Taniyama Y, Yamamoto Y, Kuroki R, Kikuchi M

Abstract excerpt

Human lysozyme is made up of 130 amino acid residues and has four disulfide bonds at Cys6-Cys128, Cys30-Cys116, Cys65-Cys81, and Cys77-Cys95. Our previous results using the Saccharomyces cerevisiae secretion system indicate that the individual disulfide bonds of human lysozyme have different func...

Topics

Amino Acid Sequence
Blotting, Western
Circular Dichroism
Cysteine
Disulfides
Humans
Models, Molecular
Molecular Sequence Data
Muramidase
Mutation
Pepsin A
Peptide Mapping
Protein Conformation
Saccharomyces cerevisiae

Source

Open in PubMed

Identifiers

PMID: 2110167

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2110167-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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