Properties of mycelial aggregate-specific lectin of Pleurotus cornucopiae produced in Pichia pastoris.
cDNA of a mycelial aggregate-specific lectin of Pleurotus cornucopiae was expressed in Pichia pastoris, and the expression product was purified and characterized. The product was functional, and the hemagglutinating activity was inhibited most strongly by the addition of N-acetyl-D-galactosamine as was the native lectin. The native lectin is a glycoprotein having five glycosylation recognition signals, and the expression product showed slightly larger molecular mass than that of the native one due to further glycosylation.
Sumisa
Futoshi
F
Department of Bioresources Chemistry, Faculty of Horticulture, Chiba University, Matsudo, Japan.
Iijima
Naoto
N
Ando
Akikazu
A
Shiga
Maiko
M
Kondo
Kozue
K
Amano
Koh
K
Nagata
Yoshiho
Y
D050260:Carbohydrate Metabolism; D018076:DNA, Complementary / Q000235:genetics; D006031:Glycosylation; D006385:Hemagglutination Inhibition Tests; D037102:Lectins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D010843:Pichia / Q000235:genetics*; D020076:Pleurotus / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity
D018076:DNA, Complementary; D037102:Lectins; D011994:Recombinant Proteins