Cyanogen bromide cleavage of the two constituent polypeptide chains of ricin d

Gunki Funatsu, Shinji Yoshitake, Masanori Ide, Makoto Kimura, Masaru Funatsu

研究成果: ジャーナルへの寄稿記事

10 引用 (Scopus)

抄録

Two constituent polypeptide chains of ricin D, a highly toxic protein from castor bean seeds, were cleaved with cyanogen bromide (CNBr). Four CNBr fragments, α-CB I, α-CB II, α-CB III, and α-CB IV, were isolated from the lie (α) chain by gel filtration through BioGel P-30 and characterized. N-Terminal sequence analyses revealed that the alignment of these fragments was (α-CB I)-(α-CB IV)-(α-CB II)-(α-CB III). CNBr cleavage of Ala rø chain, followed by reduction and S-carboxymethylation, yielded four fragments, β-CB I, β-CB II, β-CB III, and β-CB IV. Methionine residue located at 5th position from N-terminus of Ala chain was found to be resistant to CNBr cleavage. Sequence analyses of these fragments revealed that fragment β-CB IV was originated from fragment β-CB III by acid cleavage, not by CNBr cleavage of as party 1-prolyl bond d uring CNBr treatment, and the alignment of CNBr fragments was established to be (β-CB II)-(β-CB I)-(β-CB III).

元の言語英語
ページ(範囲)1253-1260
ページ数8
ジャーナルAgricultural and Biological Chemistry
42
発行部数6
DOI
出版物ステータス出版済み - 1 1 1978

Fingerprint

ricin
cyanogen
Ricin
Cyanogen Bromide
bromides
polypeptides
Peptides
Sequence Analysis
Castor Bean
castor beans
Poisons
Methionine
Gel Chromatography
Seed
methionine
Seeds
Gels
gels
Acids
acids

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

これを引用

Cyanogen bromide cleavage of the two constituent polypeptide chains of ricin d. / Funatsu, Gunki; Yoshitake, Shinji; Ide, Masanori; Kimura, Makoto; Funatsu, Masaru.

:: Agricultural and Biological Chemistry, 巻 42, 番号 6, 01.01.1978, p. 1253-1260.

研究成果: ジャーナルへの寄稿記事

Funatsu, Gunki ; Yoshitake, Shinji ; Ide, Masanori ; Kimura, Makoto ; Funatsu, Masaru. / Cyanogen bromide cleavage of the two constituent polypeptide chains of ricin d. :: Agricultural and Biological Chemistry. 1978 ; 巻 42, 番号 6. pp. 1253-1260.
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abstract = "Two constituent polypeptide chains of ricin D, a highly toxic protein from castor bean seeds, were cleaved with cyanogen bromide (CNBr). Four CNBr fragments, α-CB I, α-CB II, α-CB III, and α-CB IV, were isolated from the lie (α) chain by gel filtration through BioGel P-30 and characterized. N-Terminal sequence analyses revealed that the alignment of these fragments was (α-CB I)-(α-CB IV)-(α-CB II)-(α-CB III). CNBr cleavage of Ala r{\o} chain, followed by reduction and S-carboxymethylation, yielded four fragments, β-CB I, β-CB II, β-CB III, and β-CB IV. Methionine residue located at 5th position from N-terminus of Ala chain was found to be resistant to CNBr cleavage. Sequence analyses of these fragments revealed that fragment β-CB IV was originated from fragment β-CB III by acid cleavage, not by CNBr cleavage of as party 1-prolyl bond d uring CNBr treatment, and the alignment of CNBr fragments was established to be (β-CB II)-(β-CB I)-(β-CB III).",
author = "Gunki Funatsu and Shinji Yoshitake and Masanori Ide and Makoto Kimura and Masaru Funatsu",
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N2 - Two constituent polypeptide chains of ricin D, a highly toxic protein from castor bean seeds, were cleaved with cyanogen bromide (CNBr). Four CNBr fragments, α-CB I, α-CB II, α-CB III, and α-CB IV, were isolated from the lie (α) chain by gel filtration through BioGel P-30 and characterized. N-Terminal sequence analyses revealed that the alignment of these fragments was (α-CB I)-(α-CB IV)-(α-CB II)-(α-CB III). CNBr cleavage of Ala rø chain, followed by reduction and S-carboxymethylation, yielded four fragments, β-CB I, β-CB II, β-CB III, and β-CB IV. Methionine residue located at 5th position from N-terminus of Ala chain was found to be resistant to CNBr cleavage. Sequence analyses of these fragments revealed that fragment β-CB IV was originated from fragment β-CB III by acid cleavage, not by CNBr cleavage of as party 1-prolyl bond d uring CNBr treatment, and the alignment of CNBr fragments was established to be (β-CB II)-(β-CB I)-(β-CB III).

AB - Two constituent polypeptide chains of ricin D, a highly toxic protein from castor bean seeds, were cleaved with cyanogen bromide (CNBr). Four CNBr fragments, α-CB I, α-CB II, α-CB III, and α-CB IV, were isolated from the lie (α) chain by gel filtration through BioGel P-30 and characterized. N-Terminal sequence analyses revealed that the alignment of these fragments was (α-CB I)-(α-CB IV)-(α-CB II)-(α-CB III). CNBr cleavage of Ala rø chain, followed by reduction and S-carboxymethylation, yielded four fragments, β-CB I, β-CB II, β-CB III, and β-CB IV. Methionine residue located at 5th position from N-terminus of Ala chain was found to be resistant to CNBr cleavage. Sequence analyses of these fragments revealed that fragment β-CB IV was originated from fragment β-CB III by acid cleavage, not by CNBr cleavage of as party 1-prolyl bond d uring CNBr treatment, and the alignment of CNBr fragments was established to be (β-CB II)-(β-CB I)-(β-CB III).

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