Preparative isolation of the lectin jacalin by anion-exchange high-performance liquid chromatography.
The lectin jacalin from Artocarpus integrifolia was purified to homogeneity in a single step by preparative anion-exchange high-performance liquid chromatography (HPLC). Selection of the optimum chromatographic parameters in gradient elution allowed a rapid procedure to be obtained for the qualitative and quantitative isolation of the most important alpha- and alpha'-jacalin components. A recovery of 27-33% was obtained from a total soluble extract using a polyacrylate-DEAE HPLC column. The identities of the two isolated polypeptides were established by N-terminal amino acid sequence analysis and from the IgA1 binding lectin activity.
De Simone
S G
SG
Department of Biochemistry and Molecular Biology, Oswaldo Cruz Institute, Rio de Janeiro, Brazil.
Santos
R
R
Araujo
M F
MF
Pinho
R T
RT
D000595:Amino Acid Sequence; D000837:Anion Exchange Resins; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid / Q000379:methods*; D002852:Chromatography, Ion Exchange / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D005779:Immunodiffusion; D037102:Lectins / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D037121:Plant Lectins
D000837:Anion Exchange Resins; D037102:Lectins; D037121:Plant Lectins; C043696:jacalin