Amino Acid Sequence and Some Properties of Lectin-D from the Roots of Pokeweed (Phytolacca americana)

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概要

• 論文の詳細を見る

• Two pokeweed lectins, designated PL-D1 and PL-D2, have been isolated from the roots of pokeweed (Phytolacca americana) using chitin affinity column chromatography followed by gel filtration on a Sephacryl S-200 column and fast protein liquid chromatography on a Mono-Q column, and their amino acid sequences have been analyzed. PL-D1 consists of 84 amino acid residues and has a molecular mass of 9317, while PL-D2 has an identical sequence with PL-D1 except lack of the C-terminal Leu-Thr. PL-D is composed of two chitin-binding domains, A and B, with 50% homology with each other. Both PL-Ds did not agglutinate native rabbit erythrocytes, but showed about 0.1% of the agglutinating activity of wheat germ agglutinin toward trypsin-treated erythrocytes. In the presence of β(1→4) linked oligomers of N-acetyl-D-glucosamine, which inhibit the hemagglutination, PL-D1 had an ultraviolet-difference spectrum with maxima at 292-294 nm and 284-285 nm, attributed to the red shift of the tryptophan residue, suggesting the location of tryptophan residue(s) at or near saccharide-binding site of PL-D1.

• 社団法人日本農芸化学会の論文
• 1996-08-23

著者

• FUNATSU Gunki

  Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University

• Yamaguchi K

  Kyushu Univ. Fukuoka Jpn

• Yamaguchi K

  Sagami Chemical Res. Center Kanagawa Jpn

• Yamaguchi Ken-ichi

  Laboratory Of Protein Chemistry And Engineering Faculty Of Agriculture Kyushu University

• Funatsu G

  Kyushu Univ. Fukuoka Jpn

• Funatsu Gunki

  Laboratory Of Biochemistry And ** Laboratory Of Protein Chemistry & Engineering Faculty Of Agric

• Yamaguchi Kohji

  Tonen Corporation

• MORI Ayumi

  Laboratory of Protein Chemistry and Engineering, Faculty of Agriculture, Kyushu University

• Mori Ayumi

  Grad. Sch. Of Bio-app. & Sys. Eng. Tokyo Univ. Of Agr. & Tech.

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