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Disulfide bonds are a requirement for Kell and Cartwright (Yt a ) blood group antigen integrity
Author(s) -
Branch Donald R.,
Muensch Helmut A.,
Hian Anita L. Sy Siok,
Petz Lawrence D.
Publication year - 1983
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1983.00561.x-i1
Subject(s) - dithiothreitol , antigen , disulfide bond , chemistry , denaturation (fissile materials) , microbiology and biotechnology , biochemistry , biology , immunology , enzyme , nuclear chemistry
S ummary . We have investigated the effect of dithiothreitol (DTT) upon the Kell blood group system and other red cell antigens. All Kell blood group antigens studied (K, k, Kp a , Kp b , Js a , Js b and Ku) as well as the Cartwright (Yt a ) antigen were completely denatured after treatment with DTT. The Gerbich antigen was substantially weakened but not completely denatured. The Js a and Js b antigens appear to have an exquisite sensitivity to treatment with DTT and can be completely denatured using very low concentrations (≤2 m m ) whereas other Kell system antigens require much higher concentrations of DTT for their denaturation (100–200 m m ). Of 38 other blood group antigens investigated, only the Yt a antigen was completely denatured using 200 m m DTT. Furthermore, the Yt a antigen was denatured within the same concentration range as Kell and one can speculate that this indicates some biochemical relationship between these two blood group systems. From our results, we conclude that: (1) at least two distinct disulfide (S–S) bonds are required for maintenance of the Kell blood group antigen system; (2) Js a and Js b antigens are distinctly different from other Kell system antigens based upon sensitivity to treatment with DTT; these antigens may be located on a different antigenic domain; and (3) the Yt a antigen requires at least one disulfide bond for its maintenance of antigen integrity. Although the Gerbich antigen was not completely denatured, results indicate that disulfide bonds may also be important structural determinants for these antigens.