Journal article icon

Journal article

Human monoclonal IgG isotypes differ in complement activating function at the level of C4 as well as C1q.

Abstract:

Humanized antibodies are likely to have a major role in therapy and it is important to define their interaction with physiological effectors. By comparing a matched series of chimeric human mAbs we found that igG1 was most efficient in complement lysis, although IgG3 bound more C1q. To resolve this paradox we compared the ability of human IgG1, IgG2, IgG3, IgG4, and IgE and rat IgG2b to cause C1q binding, C1 binding and activation, C4 activation, C4b binding, and C3b binding. Rat IgG2b was in...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1084/jem.168.1.127

Authors


Bindon, CI More by this author
Brüggemann, M More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Pathology Dunn School
Journal:
The Journal of experimental medicine
Volume:
168
Issue:
1
Pages:
127-142
Publication date:
1988-07-05
DOI:
EISSN:
1540-9538
ISSN:
0022-1007
URN:
uuid:259adc46-e522-48ea-a071-2105868851d9
Source identifiers:
31027
Local pid:
pubs:31027

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP