title: The alpha- and beta-subunits of the jacalins are cleavage products from a 17-kDa precursor.
abstract: The jacalins of three Artocarpus species were purified by affinity chromatography on a desialylated mucin-CNBr-Sepharose 4B column. The beta-chains and the 14 kDa alpha-chains were separated by high pressure liquid chromatography and the 17 kDa chains by preparative electrophoresis. The 17 kDa and 14 kDa chains had a similar highly conserved N-terminal sequence. The beta-chains were different for the three species and Artocarpus champeden contained two different beta-chains. CNBr cleavage of the 17 kDa polypeptide of Artocarpus tonkinensis yielded one peptide more than the 14 kDa. The N-terminal sequence of this fragment was similar to that of the beta-chain proving that this chain results from a proteolytic cleavage at the C-terminus of the 17 kDa peptide. The large heterogeneity of the beta-chains of jacalins from different species could be used as a marker for evolutionary studies on the Artocarpus family.
authors.affiliation: Laboratoire d'Enzymologie et de Chimie des Protéines, URA1334 du C.N.R.S., Université François Rabelais, Tours, France.
authors.forename: L D
authors.initials: LD
authors.lastname: Ngoc
authors.forename: M
authors.initials: M
authors.lastname: Brillard
authors.forename: J
authors.initials: J
authors.lastname: Hoebeke
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D037121:Plant Lectins; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011498:Protein Precursors / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D000596:Amino Acids; D037102:Lectins; D010455:Peptides; D037121:Plant Lectins; D010940:Plant Proteins; D011498:Protein Precursors; C043696:jacalin