Voprosy meditsinskoi khimii (ISSN 0042-8809)

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

   
Grebenshchikova O.G., Prozorovskiĭ V.N.
PubMed Id: 1759391
Year: 1991 vol: 37  issue:5  pages: 21-24
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.
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Reference: Grebenshchikova O.G., Prozorovskiĭ V.N., 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, Voprosy meditsinskoi khimii, 1991, vol: 37(5), 21-24.
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