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 Ile (α) chain by gel filtration through Bio-Gel 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 (ß) chain, followed by reduction and S-carboxymethylation, yielded four fragments, ß–CB I, ß–CB II, ß–CB III, and ß–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 ß-CB IV was originated from fragment ß-CB III by acid cleavage, not by CNBr cleavage of aspartyl-prolyl bond during CNBr treatment, and the alignment of CNBr fragments was established to be (ß-CB II)-(ß-CB I)-(ß-CB III).
| Original language | English |
|---|---|
| Pages (from-to) | 1253-1260 |
| Number of pages | 8 |
| Journal | Agricultural and Biological Chemistry |
| Volume | 42 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - Jan 1 1978 |
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All Science Journal Classification (ASJC) codes
- Biochemistry, Genetics and Molecular Biology(all)
- Agricultural and Biological Sciences(all)
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Cyanogen Bromide Cleavage of the Two Constituent Polypeptide Chains of Ricin D. / Funatsu, Gunki; Yoshitake, Shinji; Ide, Masanori; Kimura, Makoto; Funatsu, Masaru.
In: Agricultural and Biological Chemistry, Vol. 42, No. 6, 01.01.1978, p. 1253-1260.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Cyanogen Bromide Cleavage of the Two Constituent Polypeptide Chains of Ricin D
AU - Funatsu, Gunki
AU - Yoshitake, Shinji
AU - Ide, Masanori
AU - Kimura, Makoto
AU - Funatsu, Masaru
PY - 1978/1/1
Y1 - 1978/1/1
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 Ile (α) chain by gel filtration through Bio-Gel 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 (ß) chain, followed by reduction and S-carboxymethylation, yielded four fragments, ß–CB I, ß–CB II, ß–CB III, and ß–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 ß-CB IV was originated from fragment ß-CB III by acid cleavage, not by CNBr cleavage of aspartyl-prolyl bond during CNBr treatment, and the alignment of CNBr fragments was established to be (ß-CB II)-(ß-CB I)-(ß-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 Ile (α) chain by gel filtration through Bio-Gel 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 (ß) chain, followed by reduction and S-carboxymethylation, yielded four fragments, ß–CB I, ß–CB II, ß–CB III, and ß–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 ß-CB IV was originated from fragment ß-CB III by acid cleavage, not by CNBr cleavage of aspartyl-prolyl bond during CNBr treatment, and the alignment of CNBr fragments was established to be (ß-CB II)-(ß-CB I)-(ß-CB III).
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UR - http://www.scopus.com/inward/citedby.url?scp=85004208795&partnerID=8YFLogxK
U2 - 10.1271/bbb1961.42.1253
DO - 10.1271/bbb1961.42.1253
M3 - Article
AN - SCOPUS:85004208795
VL - 42
SP - 1253
EP - 1260
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 6
ER -