Blood group A active glycoproteins of respiratory mucus and their synthesis by an N-acetylgalactosaminyltransferase.
作者： Alan P. Baker , Lee J. Griggs , J. Ronald Munro , Joseph A. Finkelstein
DOI: 10.1016/S0021-9258(19)44349-4
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摘要: Abstract An N-acetylgalactosaminyltransferase has been found in canine respiratory tissue which catalyzes the transfer of GalNAc from UDP-GalNAc to a blood group H substance with formation human A activity. The was dependent upon Mn2+ and stimulated several fold by Triton X-100. optimal pH between 5 6. approximate Km values for acceptor (porcine submaxillary mucin deficient residues at nonreducing end sugar chains) were 10-5 m 10-3 m, respectively. enzyme only dogs whose tracheal mucus inhibited agglutination red cells (type A) anti-A serum. In addition, mucins isolated had higher ratios GlcNAc than those did not inhibit hemagglutination. These studies indicate that glycoproteins activity are produced tissue.
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