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α‐L‐FUCOSYLTRANSFERASES RELATED TO BIOSYNTHESIS OF BLOOD GROUP SUBSTANCES IN HUMAN SALIVA
Author(s) -
Yazawa S.,
Furukawa K.
Publication year - 1980
Publication title -
international journal of immunogenetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.41
H-Index - 47
eISSN - 1744-313X
pISSN - 1744-3121
DOI - 10.1111/j.1744-313x.1980.tb00715.x
Subject(s) - saliva , fucosyltransferase , abo blood group system , fucose , biochemistry , chemistry , enzyme , microbiology and biotechnology , alpha amylase , biology , amylase , glycoprotein , immunology
Summary α‐L‐Fucosyltransferases were demonstrated in human saliva which catalyze the transfer of L‐fucose from GDP‐L‐[ 14 C]‐fucose to oligosaccharides from human milk. An α‐(1→4)‐L‐fucosyltransferase that synthesizes lacto‐ N ‐fucopentaose II and lacto‐ N ‐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 a substance was secreted. This enzyme activity was demonstrable neither in saliva samples of Le(a‐b‐) secretors nor non‐secretors. An α‐(1→2)‐L‐fucosyltransferase, that synthesizes lacto‐ N ‐fucopentaose I from lacto‐ N ‐tetraose, was detected in saliva samples from Le(a‐b+) secretors which secreted H and Le b substances and from Le(a‐b‐) secretors which secreted only H substance. An α‐(1→3)‐L‐fucosyltransferase was present in all saliva samples of different ABO and Lewis blood groups, irrespective of their ABH secretor status of the donors. The fucosyltransferases in saliva were activated by Mn ++ or Mg ++ ions, and were inhibited by ATP, GTP and EDTA. They had a broad pH optimun between pH 5.0 and 6.5.