Abstract:
:Cyanogen bromide fragments were isolated from the heavy chains of three human IgG myeloma proteins of the V(H)III subgroup, sequenced by an automated method, and localized to the variable region. Inspection of these sequences, together with corresponding stretches from both human and animal proteins (studied in other laboratories) led to the detection of two additional hypervariable regions characteristic of the V(H) segment of immunoglobulin heavy chains. These areas of hypervariability, involving heavy-chain residues 86-91 and 101-109, were separated by a region of relative constancy. The close relationship of these two hypervariable regions, and the previously described first heavy-chain hypervariable region (residues 31-37), to the first heavy-chain disulphide bridge implies that the three hypervariable areas might be in close steric approximation in native immunoglobulin molecules. Examination of the sequences of the terminal portion of V(H) of all these proteins (the segment from residue 95 to the beginning of homology region C(H)l) revealed that no subgroup-specific residues could be identified in this area. Thus, heavy-chain subgroup distinctions may not extend through the entire variable region.
journal_name
Proc Natl Acad Sci U S Aauthors
Kehoe JM,Capra JDdoi
10.1073/pnas.68.9.2019subject
Has Abstractpub_date
1971-09-01 00:00:00pages
2019-21issue
9eissn
0027-8424issn
1091-6490journal_volume
68pub_type
杂志文章abstract::The generation of high levels of new catalytic activities on natural and artificial protein scaffolds is a major goal of enzyme engineering. Here, we used random mutagenesis and selection in vivo to establish a sugar isomerisation reaction on both a natural (beta alpha)(8)-barrel enzyme and a catalytically inert chime...
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