Open AccessIsolation and Characterization of a Sialic Acid-specific Lectin from Hemolymph of the Southeast Asian Horseshoe CrabTachypleus gigas
Author(s) -
Isami Tsuboi,
Masahito Matsukawa,
Nobuyuki Sato
Publication year - 1993
Publication title -
bioscience, biotechnology, and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.57.1237
Subject(s) - lectin , hemolymph , biochemistry , sialic acid , limulus , sialoglycoproteins , horseshoe crab , molecular mass , affinity chromatography , biology , agglutinin , chemistry , microbiology and biotechnology , enzyme , paleontology
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.