ISSN:
1744-313X
Quelle:
Blackwell Publishing Journal Backfiles 1879-2005
Thema:
Biologie
,
Medizin
Notizen:
A β-galactoside α1 → 2 fucosyltransferase (H-enzyme) from human group O plasma which provides H blood group specificity to erythrocyte membranes has been purified approximately 22,000-fold by chromatography on DEAE-Sepharose CL-6B, GDP-hexanolamine-Sepharose 4B and SP-Sephadex C-50. The molecular weight of the H-enzyme was estimated to be 150,000 by gel filtration. Human group O erythrocyte membranes which had lost their H blood group activity by the action of α1 → 2 fucosidase were fucosylated by the transferase, and restored the H activity. Radioactive L-fucose appeared to be incorporated into glycolipid blood group substances of erythrocyte membranes. The activity of the α1 → 2 fucosyltransferase from human plasma, stomach mucosa, erythrocyte membranes and porcine stomach mucosa were specifically inhibited by the rabbit antiserum immunized with the preparation of human plasma H-enzyme. The anti-plasma H-enzyme antiserum did not inhibit the activities of α1 → 3 N-acetygalactosaminyltransferase (A-enzyme), α1 → 3 galactosyltransferase (B-enzyme), and β-N-acetylglucosaminide α1 → 3 and α1 → 4 fucosyltransferases from human plasma and stomach mucosa.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1111/j.1744-313X.1983.tb00347.x
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