The purification of the peptidoglycan associated protein of Shigella sonnei phase I by chromatofocusing.

Grazyna Adamus, E. Romanowska

Research output: Contribution to journalArticle

Abstract

Peptidoglycan associated protein of Shigella sonnei phase I was isolated from outer membrane and purified by chromatofocusing technique according to its isoelectric point. The preparation of the protein proved to be homogenous in SDS-gel electrophoresis. Apparent molecular weight of the protein was determined as 36,000 and isoelectric point pI 5.0.

Original languageEnglish (US)
Pages (from-to)489-492
Number of pages4
JournalArchivum Immunologiae et Therapiae Experimentalis
Volume32
Issue number4
StatePublished - 1984
Externally publishedYes

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Shigella sonnei
Peptidoglycan
Isoelectric Point
Proteins
Electrophoresis
Molecular Weight
Gels
Membranes

ASJC Scopus subject areas

  • Immunology

Cite this

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title = "The purification of the peptidoglycan associated protein of Shigella sonnei phase I by chromatofocusing.",
abstract = "Peptidoglycan associated protein of Shigella sonnei phase I was isolated from outer membrane and purified by chromatofocusing technique according to its isoelectric point. The preparation of the protein proved to be homogenous in SDS-gel electrophoresis. Apparent molecular weight of the protein was determined as 36,000 and isoelectric point pI 5.0.",
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AU - Romanowska, E.

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JO - Archivum Immunologiae et Therapiae Experimentalis

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