Abstract:
:Bivalent 7S subunits were obtained from 7 purified IgM human monoclonal anti-D antibodies with 33-63% of the total protein-retaining functional binding activity. The number of sites per red cell recognized by these subunits ranged between 9,400 and 28,500. The values are taken to indicate that a number of different epitopes on the D polypeptide are being recognized. There was competition between IgG and IgM antibodies for binding to the red cells, indicating that both classes of antibody are recognizing epitopes on the same D polypeptide. The value of the functional affinity constants for the binding of the 7S subunits varied between 1.0 and 8.8 x 10(7) M-1 and there was a 3- to 16-fold increase on reduction of the ionic strength (0.05 M NaCl). Using agglutination in microwells, the end-point of the titres for the native pentamer IgM antibodies occurred at concentrations in the range 7-26 ng/ml, with one exception where the concentration required was 165 ng/ml.
journal_name
Vox Sangjournal_title
Vox sanguinisauthors
Hughes-Jones NC,Gorick BD,Beale Ddoi
10.1111/j.1423-0410.1990.tb05021.xsubject
Has Abstractpub_date
1990-01-01 00:00:00pages
112-5issue
2eissn
0042-9007issn
1423-0410journal_volume
59pub_type
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