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Effect of sialidase on blood group specificity of hog submaxillary glycoproteins
Author(s) -
Aminoff David,
Morrow Marianne P.
Publication year - 1970
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80012-8
Subject(s) - glycoprotein , sialidase , neuraminic acid , chemistry , residue (chemistry) , agglutination (biology) , biochemistry , neuraminidase , antibody , microbiology and biotechnology , biology , enzyme , immunology
Hogs can be divided into three phenotypes A, H and In, depending on the ability of extracts of their submaxillary glands to inhibit the agglutination of human A cells with human anti‐A, and human O cells with eel‐anti‐H serum. Evidence is here provided that the inactive glycoprotein, In, represents H active glycoprotein containing additional N ‐glycolyl neuraminic acid, which stereospecifically masks the H determinant, α (1 → 2)‐L‐fucosyl residue.