[Antigenic activity of the N-terminal peptide of porcine muscle lactate dehydrogenase, obtained upon cyanogen bromide cleavage].
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%).
Alekseeva
A E
AE
Grebenshchikova
O G
OG
Potapkina
T A
TA
Prozorovskiĭ
V N
VN
D000595:Amino Acid Sequence; D000818:Animals; D003488:Cyanogen Bromide; D006868:Hydrolysis; D007202:Indicators and Reagents; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D010455:Peptides / Q000276:immunology*; D013552:Swine
D007202:Indicators and Reagents; D010455:Peptides; D007770:L-Lactate Dehydrogenase; D003488:Cyanogen Bromide
Antigennaia aktivnost' N-kontsevogo peptida laktatdegidrogenazy myshtssvin'i, poluchennogo pri bromtsianovom rasshcheplenii.