[The purification and properties of an extracellular sialo-specific lectin of Bacillus subtilis 316M].
A simple procedure is proposed for purification of lectin from the culture liquid of non-pathogenic Bacillus subtilis 316M, which includes fractionation with ammonium sulfate and rechromatography on Sepharose CL-6B. The procedure enables a 213-fold purification of lectin with a specific activity of 2560 U/mg protein and 51% recovery in activity. According to gel-filtration through Sepharose the lectin has a molecular weight of 190 kDa. It consists of two types of subunits with hemagglutinating activity. The lectin is highly specific to N-glycolylneuraminic and N-acetylneuraminic acids and fructose 1.6-biphosphate.
Lakhtin
V M
VM
Simonenko
I A
IA
Budanov
M V
MV
D000596:Amino Acids / Q000032:analysis; D001412:Bacillus subtilis / Q000378:metabolism*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006386:Hemagglutination Tests; D037102:Lectins / Q000032:analysis / Q000302:isolation & purification*; D008970:Molecular Weight; D012795:Sialoglycoproteins / Q000276:immunology*
D000596:Amino Acids; D037102:Lectins; D012795:Sialoglycoproteins
Ochistka i nekotorye svoĭstva vnekletochnogo sialospetsifichnogo lektina Bacillus subtilis 316M.