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  • Title: [Antigenic activity of the N-terminal peptide of porcine muscle lactate dehydrogenase, obtained upon cyanogen bromide cleavage].
    Author: Alekseeva AE, Grebenshchikova OG, Potapkina TA, Prozorovskiĭ VN.
    Journal: Vopr Med Khim; 1989; 35(4):66-72. PubMed ID: 2815682.
    Abstract:
    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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