The N-terminal sequence of Lactococcus lactis phosphoglucose isomerase purified by affinity chromatography differs from the other species

Masaru Nomura, Ikuyo Nakajima, Masatoshi Matsuzaki, Hiromi Kimoto, Ichirou Suzuki, Hisashi Aso

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

A specific monoclonal antibody, M3A, was produced to rapidly purify Lactococcus lactis phosphoglucose isomerase (PGI) for amino acid sequence analysis. M3A recognized the Lac. lactis PGI specifically and sensitively with both enzyme-linked immunosorbent assay and Western blot analysis. The enzyme was rapidly purified to a specific activity of 21.8 U/mg with a yield of 20% by a three-step procedure, including M3A-bound Sepharose chromatography. The specific activity of PGI was increased about 64.1-fold from the cell lysate. The molecular mass of Lac. lactis PGI was estimated to be about 50 kDa by SDS-PAGE. The N-terminal amino acid sequence of Lac. lactis PGI exhibited no significant similarity to other PGIs, except for a 52.6% identity to Bacillus stearothermophilus PGI A and PGI B. These results suggest that there might be some molecular types of PGI.

Original languageEnglish
Pages (from-to)315-320
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume341
Issue number2
DOIs
Publication statusPublished - 1997 May 15
Externally publishedYes

Keywords

  • EC 5.3.1.9
  • Lactococcus lactis
  • affinity chromatography
  • monoclonal antibody
  • phosphoglucose isomerase
  • protein sequence

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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