[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].
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.
Grebenshchikova
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D000818:Animals; D000906:Antibodies / Q000276:immunology*; D001665:Binding Sites; D002384:Catalysis; D004587:Electrophoresis, Agar Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors / Q000276:immunology* / Q000378:metabolism; D010446:Peptide Fragments / Q000276:immunology*; D011817:Rabbits; D051381:Rats; D013045:Species Specificity; D013552:Swine
D000906:Antibodies; D007527:Isoenzymes; D010446:Peptide Fragments; D007770:L-Lactate Dehydrogenase
Issledovanie antigennykh osobennosteĭ izofermentov laktatdegidrogenazynekotorykh biologicheskikh vidov s pomoshch'iu antipeptidnykh antitel k fragmentu iz aktivnogo tsentra laktatdegidrogenazy-M4 svin'i.