Hemagglutination activity of lactobacillus acidophilus group lactic acid bacteria

Masahiro Yamada, Tadao Saito, Takahiro Toba, Haruki Kitazawa, Junko Uemura, Takatoshi Itoh

Research output: Contribution to journalArticlepeer-review

Abstract

The cells of 28 strains of the Lactobacillus acidophilus group were evaluated for hemagglutination (HA) activity. The activity was found in the surface layer (SL) protein fraction extracted by 2 M guanidine hydrochloride. The most SL proteins from the A group strains (L. acidophilus (A1), L. crispatus (A2), L. amylovorus (A3), and L. gallinarum (A4)) showed HA activity, but the proteins from the B group strains (L. gasseri (B1) and L.johnsonii (B2)) showed no activity. The SL proteins from the A group strains were composed in common of a main component having molecular mass of about 40-45 kDa on SDS-PAGE. The SL proteins from JCM 1034 strain that showed the highest HA activity was fractionted by CM-Toyopearl ion-exchange chromatography. The highest HA activity was detected in the major protein of 41 kDa. This protein was purified and shown to be composed of about 50% of hydrophobic amino acids. The HA activity of the protein (1034 lectin) was specifically inhibited by fetuin and bovine lactoferrin at the concentrations of 80 and 160 μg/ml, respectively. The removal of N-acetylneuraminic acid from fetuin significantly decreased the inhibitory activity.

Original languageEnglish
Pages (from-to)910-915
Number of pages6
JournalBioscience, Biotechnology and Biochemistry
Volume58
Issue number5
DOIs
Publication statusPublished - 1994 Jan 1

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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