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%).
Download PDF:  
Citation:

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.
References
 2002 (vol 48)
 2001 (vol 47)
 2000 (vol 46)
 1999 (vol 45)
 1998 (vol 44)
 1997 (vol 43)
 1996 (vol 42)
 1995 (vol 41)
 1994 (vol 40)
 1993 (vol 39)
 1992 (vol 38)
 1991 (vol 37)
 1990 (vol 36)
 1989 (vol 35)
 1988 (vol 34)
 1987 (vol 33)
 1986 (vol 32)
 1985 (vol 31)
◄        ►