[Isolation and some properties of a lectin from the venom of the Vietnamese scorpion Buthus occitanus sp].
A lectin was isolated from the venom of scorpion Buthus occitanus sp. by means of Sephadex G-50 gel filtration and CM-cellulose ion exchange chromatography. The homogeneous lectin preparation consisted of homodimeric molecules with a subunit Mr of 9.3 kDa. Glycine, alanine, and serine dominated in the lectin amino acid composition. The lectin was a glycoprotein containing 20% carbohydrates (predominantly mannose and glucose). Trypsin-treated murine erythrocytes agglutinated at the lectin concentration of 32 micrograms/ml. Hemagglutination was inhibited by carbohydrates (L-fucose > D-glucose > L-rhamnose > D-xylose). The lectin revealed no phospholipase or hyaluronidase, nor toxic activity.
Khoang
N A
NA
Institute of Organoelemental Compounds, Russian Academy of Sciences, ul. Vavilova 28, Moscow, 11781 Russia.
Berezin
B B
BB
Lakhtin
V M
VM
Iamskov
I A
IA
D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D012604:Scorpion Venoms / Q000737:chemistry*; D012605:Scorpions; D013050:Spectrometry, Fluorescence
D037102:Lectins; D012604:Scorpion Venoms
Vydelenie i nekotorye svoĭstva lektina iz iada V'etnamskogo skorpiona Buthus occitanus sp.