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Article

Accelerated secretion of human lysozyme with a disulfide bond mutation.

European journal of biochemistry - 15 Apr 1992

Omura F, Otsu M, Kikuchi M

Abstract excerpt

The mutant human lysozyme, [Ala77, Ala95]lysozyme, in which the disulfide bond Cys77-Cys95 is eliminated, is known to exhibit increased secretion in yeast, compared to wild-type human lysozyme [Taniyama, Y., Yamamoto, Y., Nakao, M., Kikuchi, M. & Ikehara, M. (1988) Biochem. Biophys. Res. Commun....

Topics

Adenocarcinoma
Alanine
Amino Acid Sequence
Animals
Base Sequence
Cell Line
Cloning, Molecular
Disulfides
Gene Expression
Genes, Synthetic
Humans
Kinetics
L Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mice

Molecular Sequence Data

Muramidase

Mutation

Oligodeoxyribonucleotides

Source

Identifiers

PMID: 1572356
DOI: 10.1111/j.1432-1033.1992.tb16812.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1572356-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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Accelerated secretion of human lysozyme with a disulfide bond mutation.PMID 1572356Read ↗

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The crystal structure of a mutant human lysozyme C77/95A with increased secretion efficiency in yeast.Semantic proximity Read ↗

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