Hemagglutination Activity of Lactobacillus acidophilus Group Lactic Acid Bacteria

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

研究成果: Article査読

18 被引用数 (Scopus)

抄録

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 2m 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 160μg/ml, respectively. The removal of N-acetylneuraminic acid from fetuin significantly decreased the inhibitory activity.

本文言語English
ページ(範囲)910-915
ページ数6
ジャーナルBioscience, Biotechnology, and Biochemistry
58
5
DOI
出版ステータスPublished - 1994 1 1

ASJC Scopus subject areas

  • バイオテクノロジー
  • 分析化学
  • 生化学
  • 応用微生物学とバイオテクノロジー
  • 分子生物学
  • 有機化学

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