Purification and characterization of a carbohydrate-binding peptide from Bauhinia purpurea lectin.
In order to examine the correlation between the amino acid sequence and sugar binding specificity of Bauhinia purpurea lectin (BPA), a galactose and lactose binding lectin, a peptide which interacts with lactose was purified from an Asp-N endoproteinase digest of BPA by means of affinity chromatography on a column of lactose-Sepharose. The amino acid sequence of this peptide is Asp-Thr-Trp-Pro-Asn-Thr-Glu-Trp-Ser. A tryptic fragment having the ability to interact with lactose was also purified and found to contain the above sequence, consisting of 9 amino acids. The chemical synthesis of this peptide was carried out by the solid-phase method and the synthetic peptide was found to exhibit lactose binding activity in the presence of calcium.
Yamamoto
K
K
Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Konami
Y
Y
Kusui
K
K
Osawa
T
T
D000595:Amino Acid Sequence; D002241:Carbohydrates; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010455:Peptides / Q000302:isolation & purification*; D010835:Phytohemagglutinins / Q000737:chemistry; D037121:Plant Lectins; D012689:Sequence Homology, Nucleic Acid
C039340:Bauhinia purpurea lectin; D002241:Carbohydrates; D037102:Lectins; D010446:Peptide Fragments; D010455:Peptides; D010835:Phytohemagglutinins; D037121:Plant Lectins