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Title: [Antigenic properties of lactate dehydrogenase isoenzymes of various biological types using antipeptide antibodies to a fragment of the active center of swine lactate dehydrogenase-M4]. Author: Grebenshchikova OG, Prozorovskiĭ VN. Journal: Vopr Med Khim; 1991; 37(5):21-4. PubMed ID: 1759391. Abstract: Antigenic properties of human, pig, rabbit and rat lactate dehydrogenase (LDH) M4-isozyme as well as of human LDH-C4 were studied using antipeptide antibodies against pig LDH-M4 fragment (180-214). Amino acid sequence 180-214, containing His-195, which is involved in the active site of LDH isozymes, proved to be total antigenic determinant only for human and pig M4-isozymes. Amino acid sequence of total antigenic determinant did not allow any substitutions of essential amino acid residues. His-195, participating in substrate binding, was not involved immediately in reactions with antibodies as shown by means of chemical modification of pig M4-isozyme with diethyl pyrocarbonate and after production of antibodies against the modified isoenzyme.[Abstract] [Full Text] [Related] [New Search]