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Article

Participation of cysteine 30 residue in the folding process of ovalbumin evaluated in a refolding experiment using cysteine mutants.

Biochemical and biophysical research communications - 1 Jan 2018

Ishimaru Takayuki, Ito Kazunari, Tanaka Miho, Matsudomi Naotoshi

Abstract excerpt

To understand the role of cysteine (SH) residues in the folding of hen ovalbumin (OVA), SH-mutated OVAs, in which each SH residue was replaced by alanine (C11A, C30A, C367A, and C382A), were prepared. SDS-PAGE analysis under non-reducing conditions showed that the C11A and C30A mutants produced a disulfide (SS) isomer in addition to a protein with a native SS bond (Cys73-Cys120). The susceptibility to elastase...

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PMID: 29175210
DOI: 10.1016/j.bbrc.2017.11.146

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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