Characterization of isolectins inTetracarpidium conophorum seeds (Nigerian walnut) View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-08

AUTHORS

Theresa Animashaun, R. Adetoro Togun, R. Colin Hughes

ABSTRACT

A lectin preparation obtained from Tetracarpidium conophorum (Nigerian walnut) by affinity chromatography of seed extracts on lactose-agarose has been shown to contain two components by gel filtration on Sephadex G150. The larger component Tetracarpidium conophorum agglutinin I (TCAI) is a disulphide-bonded 70 kDa homodimer whereas the second component TCAII is a 34 kDa monomeric protein. Amino terminal aminoacid sequencing shows identity in TCAI and TCAII for the first fifteen residues after which the sequences diverge. The N-terminal sequences of TCAI and TCAII show identity with sequences in the B-chains of ricin and Ricinus communis agglutinin I (RCAI) in eleven of the initial fifteen residues. Thereafter TCAI appears to be homologous to the ricin B chain whereas TCAII is more homologous with the B chain of RCAI. A limited screening of the carbohydrate-binding specificity of TCAII by affinity chromatography of defined oligosaccharides on TCAII Sepharose columns shows that the binding specificity reported earlier for affinity purified Tetracarpidium conophorum isolectins (Sato S, Animashaun T, Hughes RC (1991) J Biol Chem 266:11485-94) reflects the binding properties of TCAII which is the major isolectin in unfractionated lectin preparations. More... »

PAGES

299-303

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00731202

DOI

http://dx.doi.org/10.1007/bf00731202

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1022000980

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7873925


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