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Identification and Purification of the Human Myeloid Differentiation Antigen Recognized by Monoclonal Antibody AHN‐7
Author(s) -
Skubitz Keith M.,
Weisdorf Daniel J.,
August J. Thomas
Publication year - 1987
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.41.2.104
Subject(s) - monoclonal antibody , biology , antigen , myeloid , microbiology and biotechnology , antibody , myeloid leukemia , leukemia , granulocyte , immunology
This report describes the characterization and expression of a human myeloid differentiation antigen defined by use of an IgG 1 monoclonal antibody (AHN‐7). This antibody binds to many granulocytic precursors in normal marrow, to most but not all granulocyte‐macrophage progenitors (CFU‐GM), and to approximately half of nonlymphoid leukemia specimens. The protein antigens recognized by AHN‐7 were purified from 35 S‐labelled HL‐60 cells by antibody affinity column chromatography. The molecule reacting with AHN‐7 was markedly heterogeneous, appearing as several forms ranging in pl from 4.5 to 6.4 with apparent molecular weights from 43,000 to 68,000. The molecules were not disutfide‐linked. Proteins bearing the antigen were minor components of the plasma membrane. The antigen was expressed by normal human peripheral blood neutrophils, monocytes, eosinophils, and basophils, and weakly on a small percentage of lymphocytes; it was not detected in red blood cells, platelets, or the majority of lymphocytes. The antibody also bound to a variety of human myeloid leukemia cell lines but not to any lymphoid leukemia cell line tested. AHN‐7 had no effect on several in vitro neutrophil functions tested.