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The Importance of Non‐Charged Amino Acids in Antibody Binding to Humicola lanuginosa Lipase
Author(s) -
NAVER H.,
LØVBORG U.
Publication year - 1995
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1995.tb03590.x
Subject(s) - epitope , antigenicity , lipase , polyclonal antibodies , antibody , amino acid , biochemistry , chemistry , enzyme , microbiology and biotechnology , site directed mutagenesis , mutagenesis , biology , mutation , mutant , genetics , gene
The antigenicity of 36 Humicola lanuginosa lipase (HL) variants, generated by site directed mutagenesis, was compared with that of the unchanged enzyme. Polyclonal antibodies raised against variant lipases were investigated and compared with the antibodies raised against the wild type lipase in an ELISA competition assay. The results showed that exchange of charged amino acids with polar residues in surface epitopes of HL, results in a tighter binding of the antibody to the epitope. Four amino acids (Trp at position 89, Asp at positions 96 and 254 and Phe at position 211) were found to be essential for antibody binding in each their epitope of the wild type enzyme.