Generation and Characterization of @entity1 Single-Chain Antibodies Against XXXX .

@entity1 @entity3406 @entity2555 @entity21807 @entity2556 @entity9437 @entity2612 @entity9435 @entity10390 @entity12684 @entity3689 @entity526
@entity2555 ( @entity2556 ) are widely distributed and relocated in the environment as a result of the incomplete combustion of organic matter. Many @entity2556 and their @entity21807 are highly toxic, mutagenic and/or carcinogenic to microorganisms as well as to higher systems including @entity1 . BP is one of the most toxicologically active @entity2556 and is often used as a prototype for this entire class of contaminants. In order to select anti-BP antibodies, the conjugate of BP with BSA (BP-BSA) was used to screen na  ve combinatorial phage library of @entity1 scFvs. Seven unique scFvs against BP-BSA were selected after three rounds of selection. Analysis of the genes encoding the scFvs subdivided them to gene families and subfamilies. Homology with the closest germline ranged from 80.21% to 97.57% for heavy chains and 88.89% to 98.57% for the light chains. Four of the seven @entity10390 @entity3689 residues sequences without stop codons in frame were selected for proteomic analysis with each other. Four scFvs encoded unique non-related proteins with low-sequence identity among them. All CDRs and the boundaries in the @entity2612 formation were carried out. Two of the scFvs (T68 and T72) with the highest binding capabilities to @entity2556 were expressed in @entity526 and purified using a @entity3406 resin. The KDs of T68 to BP-BSA, @entity12684 , @entity9435 , and @entity9437 were almost similar, approximately 10(-7   )M. The KDs of T72 to @entity9437 and @entity12684 were 9.42   *   10(-8   )M and 2.63   *   10(-7   )M, respectively. The computational models of T68 and T72 active centers were different.
