Purification and properties of a lectin from ascomycete mushroom, Ciborinia camelliae.
A lectin was isolated from an ascomycete mushroom, Ciborinia camelliae which was specific to N-acetyl-D-galactosamine. On SDS-polyacrylamide gel electrophoresis; this lectin gave a single band of approximately 17-kDa in the presence of 2-mercaptoethanol, but formed dimers, trimers and tetramers in its absence. Amino acid analysis revealed the lectin contained two cysteines and no methionine. The N-terminal sequence was determined up to residue 21, and no homologous proteins including other ascomycete lectins were found.
Otta
Yumi
Y
Department of Bioresources Chemistry, Faculty of Horticulture, Chiba University, 271-8510, Matsudo, Japan.
Amano
Koh
K
Nishiyama
Kano
K
Ando
Akikazu
A
Ogawa
Shigeru
S
Nagata
Yoshiho
Y
D000363:Agaricales / Q000737:chemistry*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D050260:Carbohydrate Metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes; D006386:Hemagglutination Tests; D006863:Hydrogen-Ion Concentration; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D008969:Molecular Sequence Data; D011817:Rabbits; D013379:Substrate Specificity; D013696:Temperature
D000596:Amino Acids; D037102:Lectins