Alteration of the carbohydrate-binding specificity of the Bauhinia purpurea lectin through the preparation of a chimeric lectin.
A chimeric lectin gene was constructed by using a cDNA clone coding the Bauhinia purpurea lectin (BPA) in which a part of the metal-binding region was replaced by the corresponding region of the mannose-binding Lens culinaris lectin (LCA). The chimeric lectin expressed in Escherichia coli was found to bind alpha mannosyl-bovine serum albumin (BSA) and this binding was inhibited by mannose.
Yamamoto
K
K
Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University of Tokyo.
Konami
Y
Y
Osawa
T
T
Irimura
T
T
D000595:Amino Acid Sequence; D001483:Base Sequence; D050260:Carbohydrate Metabolism; D002846:Chromatography, Affinity; D004926:Escherichia coli / Q000235:genetics; D037102:Lectins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008358:Mannose / Q000378:metabolism* / Q000494:pharmacology; D008969:Molecular Sequence Data; D037121:Plant Lectins; D010957:Plasmids; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012709:Serum Albumin; D012710:Serum Albumin, Bovine / Q000378:metabolism*
C039340:Bauhinia purpurea lectin; D037102:Lectins; D037121:Plant Lectins; D011993:Recombinant Fusion Proteins; D012709:Serum Albumin; C033619:lentil lectin; C023840:mannose-bovine serum albumin conjugate; D012710:Serum Albumin, Bovine; D008358:Mannose