Df. Stroncek et al., POLYCLONAL ANTIBODIES AGAINST THE NB1-BEARING 58-KDA TO 64-KDA GLYCOPROTEIN OF HUMAN NEUTROPHILS DO NOT IDENTIFY AN NB2-BEARING MOLECULE, Transfusion, 33(5), 1993, pp. 399-404
The neutrophil-specific NB antigen system has been serologically chara
cterized with human alloantisera. Two alleles, NB1 and NB2, have been
described; however, there may be important quantitative or qualitative
variation in the expression of NB1 and NB2. Human alloantibodies have
been used to identify the 58- to 64-kDa glycoprotein (GP) on which NB
1 antigen is located, but an NB2 antigen-bearing molecule has not yet
been identified. To identify the NB2 molecule, human alloantibody to N
B1 was used to isolate the 58- to 64-kDa NB1 GP, and rabbits were immu
nized with this GP. Two rabbit antisera were produced. Both antisera i
mmunoblotted and immunoprecipitated the 58- to 64-kDa GP on which NB1
is located, but neither identified the molecule on which NB2 is locate
d. The inability of two rabbit polyclonal antibodies specific for the
NB1 molecule to react with the NB2-bearing molecule suggests that cons
iderable differences may exist between these two molecules or that NB2
as currently defined is not related to NB1.