One-step purification of an alpha(1-3)-L-fucosyltransferase from human amniotic fluid by fetuin-agarose affinity chromatography.
A soluble alpha(1-3)-L-fucosyltransferase, which accepts carbohydrates of the general structure NeuAc alpha(2-3)Gal beta(1-4)GlcNAc beta-R as substrates and which is involved in the biosynthesis of the tumor-associated sialyl-LeX determinant, was purified about 125-fold from human amniotic fluid by a one-step affinity chromatography on fetuin-agarose. Upon SDS gel electrophoresis, the purified enzyme revealed a protein band with a relative molecular mass (Mr) of about 62,000. The enzyme acted equally well on sialoglycoproteins and their desialylated derivatives.
Mitsakos
A
A
Institut für Immunbiologie, Medizinische Universitätsklinik Köln.
Hanisch
F G
FG
D000653:Amniotic Fluid / Q000201:enzymology*; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005647:Fucosyltransferases / Q000302:isolation & purification*; D006602:Hexosyltransferases / Q000302:isolation & purification*; D006801:Humans; D011233:Precipitin Tests; D012685:Sepharose; D000509:alpha-Fetoproteins
D000509:alpha-Fetoproteins; D012685:Sepharose; D005647:Fucosyltransferases; D006602:Hexosyltransferases