Isolation and characterization of a sialic acid-specific lectin from hemolymph of the Southeast Asian horseshoe crab Tachypleus gigas.
A lectin was isolated from hemolymph of the Southeast Asian horseshoe crab Tachypleus gigas by using glycophorin HA affinity chromatography and Sephacryl S-300 gel filtration. The purified lectin had a molecular mass of approximately 396kDa and was composed of 13 identical subunits with molecular masses of 31 kDa. The serological specificity of the purified lectin was specifically inhibited by sialic acids sialoglycoproteins, but not by neutral sugars, hexosamines, N-acetylhexosamines, or asialoglycoproteins. Although the N-terminal amino acid sequence of the lectin from T. gigas was identical to that from American horseshoe crab (liphemin) by the same purification method and cross reacted with the anti-liphemin serum, the calcium concentration of hemagglutinating activity of the purified lectin showed a smaller optimal concentration than that of liphemin.
Tsuboi
I
I
Taiyo Central Research Institute, Taiyo Fishery Co., Ltd., Ibaraki, Japan.
Matsukawa
M
M
Sato
N
N
D000595:Amino Acid Sequence; D000818:Animals; D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D005260:Female; D006458:Hemolymph / Q000737:chemistry*; D006737:Horseshoe Crabs / Q000737:chemistry*; D037102:Lectins / Q000097:blood / Q000737:chemistry / Q000302:isolation & purification*; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D019158:N-Acetylneuraminic Acid; D012699:Serology; D063265:Sialic Acid Binding Immunoglobulin-like Lectins; D012794:Sialic Acids / Q000378:metabolism*
D037102:Lectins; D063265:Sialic Acid Binding Immunoglobulin-like Lectins; D012794:Sialic Acids; D019158:N-Acetylneuraminic Acid