Hemagglutination activity of lactobacillus acidophilus group lactic acid bacteria

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

doi:10.1080/bbb.58.910

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 journal › Article › peer-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 language	English
Pages (from-to)	910-915
Number of pages	6
Journal	Bioscience, Biotechnology and Biochemistry
Volume	58
Issue number	5
DOIs	https://doi.org/10.1080/bbb.58.910
Publication status	Published - 1994 Jan 1

ASJC Scopus subject areas

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

Access to Document

10.1080/bbb.58.910

Cite this

@article{df2131d96d434bbfb418c71d5588a478,

title = "Hemagglutination activity of lactobacillus acidophilus group lactic acid bacteria",

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.",

author = "Masahiro Yamada and Tadao Saito and Takahiro Toba and Haruki Kitazawa and Junko Uemura and Takatoshi Itoh",

year = "1994",

month = jan,

day = "1",

doi = "10.1080/bbb.58.910",

language = "English",

volume = "58",

pages = "910--915",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "5",

}

TY - JOUR

T1 - Hemagglutination activity of lactobacillus acidophilus group lactic acid bacteria

AU - Yamada, Masahiro

AU - Saito, Tadao

AU - Toba, Takahiro

AU - Kitazawa, Haruki

AU - Uemura, Junko

AU - Itoh, Takatoshi

PY - 1994/1/1

Y1 - 1994/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0028425467&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028425467&partnerID=8YFLogxK

U2 - 10.1080/bbb.58.910

DO - 10.1080/bbb.58.910

M3 - Article

C2 - 7517228

SN - 0916-8451

VL - 58

SP - 910

EP - 915

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 5

ER -

Hemagglutination activity of lactobacillus acidophilus group lactic acid bacteria

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this