Biochemical similarity among serologically distinct flagellins of Campylobacter jejuni

Irving Nachamkin, Ruth Hogue Angeletti, Michael B. Prystowsky

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

We describe a simplified method for obtaining highly purified flagellin, suitable for biochemical analysis using HPLC-gel permeation. Amino acid composition and N-terminal sequence analyses were performed on flagellins from serologically distinct isolates. The amino acid composition of flagellin from 10 strains was very similar. The N-terminal amino acid sequence is highly conserved. Significant sequence homology was found with flagellin of Bacillus subtilis.

Original languageEnglish (US)
Pages (from-to)149-152
Number of pages4
JournalFEMS Microbiology Letters
Volume51
Issue number2-3
StatePublished - Jun 15 1988
Externally publishedYes

Fingerprint

Flagellin
Campylobacter jejuni
Amino Acids
Sequence Homology
Bacillus subtilis
Sequence Analysis
Amino Acid Sequence
Gels
High Pressure Liquid Chromatography

Keywords

  • (Amino acid sequence)
  • (HPLC-gel permeation)
  • Campylobacter jejuni
  • Flagellin

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Applied Microbiology and Biotechnology
  • Microbiology

Cite this

Biochemical similarity among serologically distinct flagellins of Campylobacter jejuni. / Nachamkin, Irving; Angeletti, Ruth Hogue; Prystowsky, Michael B.

In: FEMS Microbiology Letters, Vol. 51, No. 2-3, 15.06.1988, p. 149-152.

Research output: Contribution to journalArticle

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