Isolation and Amino Acid Sequence of a Protein-synthesis Inhibitor from the Seeds of Rye (Secale cereale) | Zendy

Yuji Minami | Zendy; Kenichi Yamaguchi | Zendy; Fumio Yagi | Zendy; Kenjiro Tadera | Zendy; Gunki Funatsu | Zendy

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Isolation and Amino Acid Sequence of a Protein-synthesis Inhibitor from the Seeds of Rye (Secale cereale)

Author(s) -

Yuji Minami,

Kenichi Yamaguchi,

Fumio Yagi,

Kenjiro Tadera,

Gunki Funatsu

Publication year - 1998

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.62.1152

Subject(s) - secale , ricin , isoelectric point , cyanogen bromide , biochemistry , amino acid , peptide sequence , biology , size exclusion chromatography , chemistry , chromatography , enzyme , botany , gene , toxin

A protein-synthesis inhibitor, designated RPSI, was isolated from the seeds of rye (Secale cereale) using gel filtration and S-Sepharose column chromatography. RPSI is a basic protein with an isoelectric point of over 10, and the concentration of protein required for 50% inhibition of protein synthesis (IC50) of purified RPSI was about ten-fold the concentration of ricin A-chain. The complete amino acid sequence of RPSI was discovered by analyzing the peptides and fragments obtained from the proteolytic digests and by the cyanogen bromide- and hydroxylamine-cleavages of RPSI. RPSI consists of 280 amino acid residues and has a molecular weight of 30,171. RPSI has only 21% sequence identity with that of ricin A-chain, but all five amino acid residues involved in the active site of ricin A-chain are conserved in RPSI.

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