VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Antigenic activity of the N-terminal peptide of porcine muscle lactate dehydrogenase, obtained upon cyanogen bromide cleavage

   
Alekseeva A.E., Grebenshchikova O.G., Potapkina T.A., Prozorovskiĭ V.N.
PubMed Id: 2815682
Year: 1989  Volume: 35  Issue: 4  Pages: 66-72
N-terminal peptide was isolated from BrCN hydrolysate of pig muscle lactate dehydrogenase (LDH), its antigenic properties were studied using solid-phase immunoenzyme assay. N-terminal fragment containing 1-32 amino acids of LDH exhibited the antigenic activity towards antiserum and specific antibodies to native LDH5 and inhibited formation of the antigen-antibody complex by 25-35%, thus suggesting the presence of at least one antigenic determinant in the N-terminal fragment. The N-terminal peptide of LDH5 conjugated with bovine albumin maintained the antigenic activity towards specific antibodies against native LDH5 (inhibition by 20-25%).
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Alekseeva, A. E., Grebenshchikova, O. G., Potapkina, T. A., Prozorovskiĭ, V. N. (1989). Antigenic activity of the N-terminal peptide of porcine muscle lactate dehydrogenase, obtained upon cyanogen bromide cleavage. Voprosy meditsinskoi khimii, 35(4), 66-72.
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