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. 1986 Oct;83(19):7256–7260. doi: 10.1073/pnas.83.19.7256

Identification and purification of a bacterial ice-nucleation protein.

P K Wolber, C A Deininger, M W Southworth, J Vandekerckhove, M van Montagu, G J Warren
PMCID: PMC386694  PMID: 3020542

Abstract

The protein product of a gene (inaZ) responsible for ice nucleation by Pseudomonas syringae S203 has been identified and purified after overexpression in Escherichia coli. The amino acid composition and the N-terminal sequence of the purified, denatured protein corresponded well with that predicted from the sequence of the inaZ gene. The product of inaZ was also found to be the major component in preparations of ice-nucleating, proteinaceous particles, obtained after extraction with and gel filtration in a mixture of urea and the nondenaturing detergent octyl beta-D-thioglucopyranoside. The activity of these preparations in the absence of added lipid implies that the protein participates directly in the nucleation process.

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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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