Literature DB >> 16664561

Lectins in castor bean seedlings.

S M Harley1, H Beevers.   

Abstract

The amounts of the two lectins (ricin and Ricinus communis agglutinin) in tissues of castor bean seedlings were followed during germination and early growth. For measurement, lectins in extracts were separately eluted from Sepharose columns; an antibody to the agglutinin was also used to detect the lectins by immunodiffusion. The endosperm of the dry seed contains 3.5 mg total lectin (5.6% of the total seed protein), which declines by 50% by day 4 and more rapidly thereafter as the tissue is completely consumed. The cotyledons of the dry seed also contain lectins but the amounts are less than 1% of those in the endosperm, and, as in the endosperm, they are constituents of the albumin fraction of the isolated protein bodies. No lectins were detected in the green cotyledons of 10-day seedlings that had been exposed to light from day 5. The embryonic axes of 2-day seedlings contained very small amounts of lectins but they were not detectable in the aerial parts of seedlings grown for 3 weeks or in cells from endosperm grown in tissue culture.The ability of proteinases and glycosidases (isolated from endosperm of 4-day seedlings) to hydrolyze the lectins was examined. No hydrolysis of the two lectins was observed, but the subunits, separated by reduction with 2-mercaptoethanol, were hydrolyzed slowly by a proteinase and some release of mannose was observed in the presence of the glycosidases. Ricin was converted to its subunits by cysteine and an enzyme in an endosperm extract accelerated chain separation by glutathione.

Entities:  

Year:  1986        PMID: 16664561      PMCID: PMC1075046          DOI: 10.1104/pp.80.1.1

Source DB:  PubMed          Journal:  Plant Physiol        ISSN: 0032-0889            Impact factor:   8.340


  32 in total

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3.  Structure and toxicity of pure ricinus agglutinin.

Authors:  E Saltvedt
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4.  Purification by immunoadsorbtion chromatography of the normal and a mutant form of the B2 subunit of Escherichia coli tryptophan synthase.

Authors:  L M Shannon; S E Mills
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Authors:  J Howard; J Kindinger; L M Shannon
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6.  Conformation-dependent antigenic determinants in the toxic lectin ricin.

Authors:  S Olsnes; E Saltvedt
Journal:  J Immunol       Date:  1975-06       Impact factor: 5.422

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Authors:  M Nishimura
Journal:  Plant Physiol       Date:  1982-09       Impact factor: 8.340

8.  Studies on the structure and properties of the lectins from Abrus precatorius and Ricinus communis.

Authors:  S Olsnes; K Refsnes; T B Christensen; A Pihl
Journal:  Biochim Biophys Acta       Date:  1975-09-09

9.  Isolation and properties of a lectin from sainfoin (Onobrychis viciifolia, Scop.).

Authors:  K D Hapner; J E Robbins
Journal:  Biochim Biophys Acta       Date:  1979-09-29

10.  Effect of sulfhydryl reagents and protease inhibitors on sodium dodecyl sulfate-heat induced dissociation of Ricinus communis agglutinin.

Authors:  D B Cawley; L L Houston
Journal:  Biochim Biophys Acta       Date:  1979-11-23
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