STUDIES ON FUCOSYLTRANSFERASES RELATED TO BIOSYNTHESIS OF HUMAN BLOOD GROUP SUBST ANCES:I. FUCOSYLTRANSFERASES IN HUMAN SALIVA
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Focosyltransferases catalize the transfer of <SUP>14</SUP>C-fucose from GDP-L-fucose-<SUP>14</SUP>C to oligosaccharides from human milk were demonstrated in human saliva.<BR>1) An α- (1→4) -fucosyltransferase that synthesizes lacto-<I>N</I>-fucopentaose II and lacto-<I>N</I>-difucohexaose I from lacto-N-tetraose and lacto-N-fucopentaose I, respectively, was detected in saliva samples of Le (a-b+) secretors and Le (a+b-) non-secretors in which Le<SUP>a</SUP> substance was secreted.<BR>This enzyme activity was not detectable in saliva samples of Le (a-b-) secretors and nonsecretors, in which Le<SUP>a</SUP> substance was absent.<BR>2) An α- (1→2) -fucosyltransferase that synthesizes lacto-<I>N</I>-fucopentaose I from lacto-<I>N</I>-tetraose, was detected in saliva samples from Le (a-b+) secretors, secreted H and Le<SUP>b</SUP> substances, and from Le (a-b-) secretors, secreted only H substance.<BR>3) An α- (1→3) -fucosyltransferase was detected in all saliva samples from donors of different ABO and Lewis blood groups irrespective of their ABH secretor status.<BR>4) The fucosyltransferases were activated by Mn<SUP>++</SUP> or Mg<SUP>++</SUP> ions, and was inhibited completely with ATP, GTP and EDTA. They had a broad pH optimum between 5.0 and 7.0.<BR>5) Lacto-<I>N</I>-difucohexaose I could be synthesized from lacto-<I>N</I>-fucopentaose I by theα- (1→4) -fucosyltransferase from a saliva of OLe (a-b+) sec.donor.The difucohexaose could not be synthesized from lacto-<I>N</I>-fucopentaose II by the α- (1→2) -fucosyltransferase. Concerning the substrate specificities of the enzymes, it was, therefore, confirmed that H antigens could be converted to Le<SUP>b</SUP> antigens.
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