Hemagglutination Activity of<i>Lactobacillus acidophilus</i>Group Lactic Acid Bacteria
書誌事項
- タイトル別名
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- Hemagglutination Activity of Lactobacillus acidophilus Group Lactic Acid Bacteria.
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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.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 58 (5), 910-915, 1994
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681453109632
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- NII論文ID
- 110002676971
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- NII書誌ID
- AA10824164
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- COI
- 1:CAS:528:DyaK2cXktlSlurk%3D
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- ISSN
- 13476947
- 09168451
- http://id.crossref.org/issn/09168451
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- PubMed
- 7517228
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可