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. 1989 Aug 15;262(1):103–107. doi: 10.1042/bj2620103

Ovalbumin and angiotensinogen lack serpin S-R conformational change.

P E Stein 1, D A Tewkesbury 1, R W Carrell 1
PMCID: PMC1133235  PMID: 2818556

Abstract

Cleavage of ovalbumin and angiotensinogen at sites homologous to the reactive centre loop of alpha 1-antitrypsin is not accompanied by the increase in heat-stability associated with the transition from the native stressed (S) structure to a cleaved relaxed (R) form that is typical of other serpins. Failure to undergo the S-R change in ovalbumin is not due to phosphorylation of Ser-344 near the sites of cleavage on the loop. The suggested explanation is the unique presence of bulky side chains at the P10-P12 site in ovalbumin and angiotensinogen.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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