Purification, characterization, and amino acid sequence of an embryonic lectin in perivitelline fluid of the horseshoe crab

Taku Nagai, Shun-Ichiro Kawabata, Fumio Shishikura, Hiroaki Sugita

研究成果: ジャーナルへの寄稿記事

17 引用 (Scopus)

抄録

Hemagglutinating activity in perivitelline fluid of the horseshoe crab embryo dramatically increases during the third and fourth molt of the embryo. A 27-kDa lectin, which we named tachylectin-P (TL-P), was newly identified in perivitelline fluid of the horseshoe crab Tachypleus tridentatus. TL-P preferentially agglutinated human A-type erythrocytes, and the activity was inhibited by N-acetyl group-containing monosaccharides. The amino acid sequence analysis indicated that TL-P is almost structurally the same as a hemocyte-derived lectin with no hemagglutinating activity, tachylectin-1 (TL- 1), and that 218 out of 221 amino acid residues in total were conserved between the two lectins. Despite the high sequence similarity, biological and biochemical characteristics of TL-P differed from those of TL-1: (i) unlike TL-1, TL-P agglutinates several animal-derived erythrocytes; (ii) unlike TL- 1, TL-P has no significant affinity for bacterial lipopolysaccharides or antibacterial activity; (iii) Based on apparent molecular masses determined by gel filtration, TL-P forms a dimer in solution, while TL-1 is present as a monomer; (iv) and TL-P interacts with endogenous proteins of 13 and 14 kDa present in the perivitelline fluid; however, neither has any affinity for TL- 1. We propose that TL-P may have an important role in completing embryonic development by interacting with endogenous glycoproteins or N- acetylhexosamines.

元の言語英語
ページ(範囲)37673-37678
ページ数6
ジャーナルJournal of Biological Chemistry
274
発行部数53
DOI
出版物ステータス出版済み - 12 31 1999

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Horseshoe Crabs
Lectins
Purification
Amino Acid Sequence
Amino Acids
Fluids
Embryonic Structures
Erythrocytes
Tachypleus tridentatus tachylectin P
Hemocytes
Monosaccharides
Protein Sequence Analysis
Molecular mass
Dimers
Embryonic Development
Gel Chromatography
Lipopolysaccharides
Glycoproteins
Animals
Monomers

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Purification, characterization, and amino acid sequence of an embryonic lectin in perivitelline fluid of the horseshoe crab. / Nagai, Taku; Kawabata, Shun-Ichiro; Shishikura, Fumio; Sugita, Hiroaki.

:: Journal of Biological Chemistry, 巻 274, 番号 53, 31.12.1999, p. 37673-37678.

研究成果: ジャーナルへの寄稿記事

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abstract = "Hemagglutinating activity in perivitelline fluid of the horseshoe crab embryo dramatically increases during the third and fourth molt of the embryo. A 27-kDa lectin, which we named tachylectin-P (TL-P), was newly identified in perivitelline fluid of the horseshoe crab Tachypleus tridentatus. TL-P preferentially agglutinated human A-type erythrocytes, and the activity was inhibited by N-acetyl group-containing monosaccharides. The amino acid sequence analysis indicated that TL-P is almost structurally the same as a hemocyte-derived lectin with no hemagglutinating activity, tachylectin-1 (TL- 1), and that 218 out of 221 amino acid residues in total were conserved between the two lectins. Despite the high sequence similarity, biological and biochemical characteristics of TL-P differed from those of TL-1: (i) unlike TL-1, TL-P agglutinates several animal-derived erythrocytes; (ii) unlike TL- 1, TL-P has no significant affinity for bacterial lipopolysaccharides or antibacterial activity; (iii) Based on apparent molecular masses determined by gel filtration, TL-P forms a dimer in solution, while TL-1 is present as a monomer; (iv) and TL-P interacts with endogenous proteins of 13 and 14 kDa present in the perivitelline fluid; however, neither has any affinity for TL- 1. We propose that TL-P may have an important role in completing embryonic development by interacting with endogenous glycoproteins or N- acetylhexosamines.",
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