Voprosy meditsinskoi khimii (ISSN 0042-8809)

Selective interaction of antipeptide antibodies to N-terminal site of lactate dehydrogenase-5 from swine muscle with various isoforms of human lactate dehydrogenase

   
Alekseeva A.E., Potapkina T.A., Prozorovskiĭ V.N.
PubMed Id: 2343581
Year: 1990 vol: 36  issue:1  pages: 73-75
Abstract: Antipeptide antibodies produced towards N-terminal site of lactate dehydrogenase-5 (LDH5) from pig muscular tissue exhibited specific reactions with N-terminal site of pig LDH5 and the whole enzyme molecule. An immunosorbent containing the antipeptide antibodies produced bound and precipitated all the LDH isoforms involving even a single M-subunit of the enzyme (LDH2, LDH5) but did not precipitate H4-isoform (LDH1) in extracts of human heart and skeletal muscle tissues and in blood serum of patients with myocardium infarction. The data obtained suggest that antipeptide antibodies against N-terminal site of pig muscular tissue LDH reacted selectively only with M-subunits of human LDH and did not interact with H4 isoform, which occurred due to dissimilarities in primary structure of N-terminal sites of M4 and H4 LDH isoenzymes.
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Reference: Alekseeva A.E., Potapkina T.A., Prozorovskiĭ V.N., Selective interaction of antipeptide antibodies to N-terminal site of lactate dehydrogenase-5 from swine muscle with various isoforms of human lactate dehydrogenase, Voprosy meditsinskoi khimii, 1990, vol: 36(1), 73-75.
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