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Ukr Biokhim Zh (1999) ; 81(3): 77-83, 2009.
Article in Ukrainian | MEDLINE | ID: mdl-19877432

ABSTRACT

Proteolytic activity of blood serum IgGs of 10 patients with systemic lupus erythematosis (SLE) was studied in comparison with such activity in 10 clinically healthy donors. Antibodies were precipitated from blood serum by saturation with 50% (NH4)2SO4 and IgG was isolated by the affinity chromatography on protein G-sepharose column. Histone H1 and core histones from the calf thymus, bovine myelin basic protein (MBP), lysozyme of chicken egg and bovine serum albumin (BSA) were used as substrates for proteolytic action. It was found that 4 of 10 preparations of IgGs possess an ability to hydrolyze both histone H1 and MBP. These antibodies practically did not cleave lysozyme of the chicken egg and BSA. Gel-filtration of antibodies under acidic condition and following examination of proteolytic activity of chromatographic fractions showed that histone H1 and MBP-hydrolyzing activity is attributable to IgG-antibodies. Thus, the presence of catalytically active antibodies (protabzymes) in the blood serum of patients with SLE has been demonstrated. Their origination and biological role are discussed.


Subject(s)
Antibodies, Catalytic/blood , Immunoglobulin G/blood , Lupus Erythematosus, Systemic/immunology , Animals , Antibodies, Catalytic/immunology , Antibodies, Catalytic/metabolism , Cattle , Chickens , Electrophoresis, Polyacrylamide Gel , Histones/metabolism , Humans , Hydrolysis , Immunoglobulin G/immunology , Immunoglobulin G/isolation & purification , Immunoglobulin G/metabolism , Lupus Erythematosus, Systemic/blood , Muramidase/metabolism , Myelin Basic Protein/metabolism , Peptide Hydrolases/metabolism
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