A novel homodimeric lactose-binding lectin from the edible split gill medicinal mushroom Schizophyllum commune.
A homodimeric lactose-binding lectin with a molecular mass of 64kDa was isolated from fresh fruiting bodies of the split gill mushroom Schizophyllum commune. The N-terminal sequence of the lectin is similar to a part of the sequence of the cell division protein from Gleobacter violaceus. The lectin was isolated by using a procedure which involved ion exchange chromatography on DEAE-cellulose, CM-cellulose, and Q-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The hemagglutinating activity of the lectin was stable at temperatures up to 40 degrees C, and in concentrations of NaOH and HCl solution up to 125 and 25mM, respectively. The lectin exhibited potent mitogenic activity toward mouse splenocytes, antiproliferative activity toward tumor cell lines, and inhibitory activity toward HIV-1 reverse transcriptase. It was devoid of antifungal activity.
Han
C H
CH
State Key Laboratory for Agrobiotechnology, Department of Microbiology, China Agricultural University, Beijing, 100094, China.
Liu
Q H
QH
Ng
T B
TB
Wang
H X
HX
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D007785:Lactose / Q000378:metabolism*; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D012567:Schizophyllum / Q000737:chemistry*
D037102:Lectins; D007785:Lactose