Description: | Catalytic antibodies, also named ‘artificial abzymes’, were first
obtained in 1986 by means of immunization of animals with
hapten analogs of the stable transition states of chemical reactions
(Pollack et al., 1986; Tramontano et al., 1986). The catalytic
antibodies revealed in the human organism were represented
by IgGs from blood serum of bronchial asthma patients and
were capable of cleaving the intestinal vasoactive peptide (Paul
et al., 1989). Such catalytic antibodies were named ‘natural
abzymes’. Properties of the natural abzymes were described in
detail in several recent reviews (Planque et al., 2008; Taguchi
et al., 2008; Belogurov et al., 2009) and book chapters (Nevinsky
and Buneva, 2005; Hanson et al., 2005; Kit et al., 2012). Abzymes
were detected in the human organism at a variety of autoimmune
and some nonautoimmune pathologies (Nevinsky and
Buneva, 2003; Gabibov et al., 2006). Various peptides, proteins,
nucleic acids and oligosaccharides can serve as substrates for
the catalytically active antibodies in humans and other mammals
(Hanson et al., 2005; Lacroix-Desmazes et al., 2006). The involvement
of abzymes in pathogenesis of the autoimmune
disorders has been demonstrated (Nevinsky and Buneva, 2005;
Hanson et al., 2005; Gabibov et al., 2006; Lacroix-Desmazes
et al., 2006). Thus, abzymes might serve as potential markers
for diagnosis of the severity of autoimmune diseases. The purification
of abzymes from mammalian biological fluids is a complicated
task because native enzyme analogs usually exist in the
mammalian body. To satisfy criteria of purity of antibodies which
belong to abzymes, a multistep procedure including sequential
ion exchange, size exclusion and affinity chromatography is
used. Affinity chromatography is a pivotal step in the purification
of abzymes, since it permits separation of antigen-specific from
antigen-unspecific antibodies. It was effectively used for purifying
from human blood serum and others biological fluids (milk,
liquor) abzymes belonging to different immunoglobulin subclasses
and possessing DNase (Shuster et al., 1992; Gololobov
et al., 1995), protease (Paul et al., 1989; Li et al., 1995; Magorivska
et al., 2010; Odintsova et al., 2011; Legostaeva et al., 2009) and
protein kinase (Kit et al., 1996; Nevinsky et al., 1998) activities.
We have shown that in the blood serum of some multiple myeloma
patients there are IgGs possessing sialidase activity (Bilyy
et al., 2011). Sialidase active IgGs were also detected in blood serum
of the systemic lupus erythematosis (SLE) patients, but they
were not found in healthy donors (Bilyy et al., 2011). Recently, we
also created artificial sialidase abzyme by means of rabbit immunization
with a synthetic hapten consisting of nonhydrolyzable
inhibitor of sialidase reaction conjugated with bovine serum |