2010/12/01 by E. P. Altshuler, Evgeny P Altshuler, D. V. Serebryanaya +3
Biochemistry, Genetics and Molecular Biology · Environmental Science · Medicine · #Bacteriophages and microbial interactions #Monoclonal and Polyclonal Antibodies Research #Protein purification and stability
paper · doi:10.1134/s0006297910130067
crossref issued 2010/12/01 · crossref published 2010/12/01 · crossref published-print 2010/12/01 · openalex publication_date 2010/12/01 · crossref published-online 2011/01/14 · crossref created 2011/02/06 · openalex created_date 2025/10/10 · crossref deposited 2026/03/15 · crossref indexed 2026/07/28 · openalex updated_date 2026/07/31
Highly specific interaction with foreign molecules is a unique feature of antibodies. Since 1975, when Keller and Milstein proposed the method of hybridoma technology and prepared mouse monoclonal antibodies, many antibodies specific to various antigens have been obtained. Recent development of methods for preparation of recombinant DNA libraries and in silico bioinformatics approaches for protein structure analysis makes possible antibody preparation using gene engineering approaches. The development of gene engineering methods allowed creating recombinant antibodies and improving characteristics of existing antibodies; this significantly extends the applicability of antibodies. By modifying biochemical and immunochemical properties of antibodies by changing their amino acid sequences it is possible to create antibodies with properties optimal for certain tasks. For example, application of recombinant technologies resulted in antibody preparation of high affinity significantly exceeding the initial affinity of natural antibodies. In this review we summarize information about the structure, modes of preparation, and application of recombinant antibodies and their fragments and also consider the main approaches used to increase antibody affinity.