Abstract：
:The amino-acid sequence of the very high-affinity anti-angiotensin II monoclonal antibody 4D8 was predicted from the nucleotide sequence of the heavy and light chain variable genes. The single-chain variable fragment (scFv) was constructed and expressed in Escherichia coli as a soluble protein and at the surface of the filamentous M13 phage and was compared with the full-length antibody (Ab). The scFv showed the same specificity profile and affinity constant as the intact antibody (5.0x10(10) and 8.0x10(10) M(-1), respectively, by Scatchard analysis). Several peptides from the set of overlapping dodecapeptides covering the variable domains of 4D8 mAb were found to specifically bind biotinylated angiotensin II: peptides from the L1, L2, L3 and H1 regions had the strongest capacity to bind the antigen.
journal_name
J Immunol Methodsjournal_title
Journal of immunological methodsauthors
Cohen P,Laune D,Teulon I,Combes T,Pugnière M,Badouaille G,Granier C,Mani JC,Simon Ddoi
10.1016/s0022-1759(01)00395-7keywords:
subject
Has Abstractpub_date
2001-08-01 00:00:00pages
147-60issue
1-2eissn
0022-1759issn
1872-7905pii
S0022175901003957journal_volume
254pub_type
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