Literature DB >> 3801493

The complete amino acid sequence of the B-chain of ricin E isolated from small-grain castor bean seeds. Ricin E is a gene recombination product of ricin D and Ricinus communis agglutinin.

T Araki, G Funatsu.   

Abstract

The complete amino acid sequence of the B-chain of ricin E has been determined. The reduced and carboxymethylated B-chain was digested with trypsin, followed by separation and purification of the resulting peptides using reverse-phase HPLC. The amino acid sequence of each tryptic peptide was determined employing the DABITC/PITC double-coupling method. The B-chain of ricin E proved to consist of 262 amino acid residues. By comparing the amino acid sequence of the B-chain of ricin E with those of ricin D and of Ricinus communis agglutinin, it was found that the B-chain of ricin E was composed of the N-terminal half of ricin D and C-terminal half R. communis agglutinin. This result suggested that the gene recombination probably occurred at the center region of two B-chain genes of ricin D and R. communis agglutinin.

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Year:  1987        PMID: 3801493     DOI: 10.1016/0167-4838(87)90008-2

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  13 in total

1.  The lectin gene family of Ricinus communis: cloning of a functional ricin gene and three lectin pseudogenes.

Authors:  J W Tregear; L M Roberts
Journal:  Plant Mol Biol       Date:  1992-02       Impact factor: 4.076

2.  Characterization of a cDNA encoding ricin E, a hybrid ricin-Ricinus communis agglutinin gene from the castor plant Ricinus communis.

Authors:  B F Ladin; E E Murray; A C Halling; K C Halling; N Tilakaratne; G L Long; L L Houston; R F Weaver
Journal:  Plant Mol Biol       Date:  1987-05       Impact factor: 4.076

3.  Crystallization and preliminary crystallographic study of oligomers of the haemolytic lectin CEL-III from the sea cucumber Cucumaria echinata.

Authors:  Hideaki Unno; Keigo Hisamatsu; Tomonao Nagao; Yuki Tateya; Naoki Matsumoto; Shuichiro Goda; Tomomitsu Hatakeyama
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-03-28

4.  Lipolytic activity of ricin from Ricinus sanguineus and Ricinus communis on neutral lipids.

Authors:  S Lombard; M E Helmy; G Piéroni
Journal:  Biochem J       Date:  2001-09-15       Impact factor: 3.857

5.  Isolation and partial characterization of nigrin b, a non-toxic novel type 2 ribosome-inactivating protein from the bark of Sambucus nigra L.

Authors:  T Girbés; L Citores; J M Ferreras; M A Rojo; R Iglesias; R Muñoz; F J Arias; M Calonge; J R García; E Méndez
Journal:  Plant Mol Biol       Date:  1993-09       Impact factor: 4.076

Review 6.  Ricinus communis intoxications in human and veterinary medicine-a summary of real cases.

Authors:  Sylvia Worbs; Kernt Köhler; Diana Pauly; Marc-André Avondet; Martin Schaer; Martin B Dorner; Brigitte G Dorner
Journal:  Toxins (Basel)       Date:  2011-10-24       Impact factor: 4.546

Review 7.  Ribosome-inactivating and related proteins.

Authors:  Joachim Schrot; Alexander Weng; Matthias F Melzig
Journal:  Toxins (Basel)       Date:  2015-05-08       Impact factor: 4.546

8.  An International Proficiency Test to Detect, Identify and Quantify Ricin in Complex Matrices.

Authors:  Sylvia Worbs; Martin Skiba; Jennifer Bender; Reinhard Zeleny; Heinz Schimmel; Werner Luginbühl; Brigitte G Dorner
Journal:  Toxins (Basel)       Date:  2015-11-26       Impact factor: 4.546

9.  Recommended Mass Spectrometry-Based Strategies to Identify Ricin-Containing Samples.

Authors:  Suzanne R Kalb; David M Schieltz; François Becher; Crister Astot; Sten-Åke Fredriksson; John R Barr
Journal:  Toxins (Basel)       Date:  2015-11-25       Impact factor: 4.546

10.  Characterization of Ricin and R. communis Agglutinin Reference Materials.

Authors:  Sylvia Worbs; Martin Skiba; Martin Söderström; Marja-Leena Rapinoja; Reinhard Zeleny; Heiko Russmann; Heinz Schimmel; Paula Vanninen; Sten-Åke Fredriksson; Brigitte G Dorner
Journal:  Toxins (Basel)       Date:  2015-11-26       Impact factor: 4.546

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