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Article

The role of the disulfide bridge in the stability and structural integrity of ovalbumin evaluated by site-directed mutagenesis.

Bioscience, biotechnology, and biochemistry - 1 Jan 2011

Ishimaru Takayuki, Ito Kazunari, Tanaka Miho, Tanaka Syunpei, Matsudomi Naotoshi

Abstract excerpt

To provide a molecular explanation of the role of the disulfide (SS) bridge in the thermostability and structural integrity of ovalbumin (OVA), we prepared SS-mutated OVAs in which SS-forming residues were replaced by Ala or Ser (C73A, C73S, C120A, and C73/120A), and compared the conformation, thermostability, susceptibility to elastase, and formation of heat-stable OVA (S-OVA) with those of the wild-type. The...

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Identifiers

PMID: 21389617
DOI: 10.1271/bbb.100772

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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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