Anti-histone H1 IgGs from blood serum of systemic lupus erythematosus patients are capable of hydrolyzing histone H1 and myelin basic protein.

Novel hydrolytic activity of the anti-histone H1 antibodies (Ab) toward histone H1 and myelin basic protein (MBP) was shown. Blood serum of ten patients with clinically diagnosed systemic lupus erythematosus (SLE), and nine healthy donors (control) were screened for the anti-histone H1 antibody- and anti-MBP antibody-mediated specific proteolytic activity. IgGs were isolated by chromatography on Protein G-Sepharose, and four of ten SLE patients appeared to possess IgGs that were capable of cleaving both histone H1 and MBP. Such activity was confirmed to be an intrinsic property of the IgG molecule, since it was preserved at gel filtration at alkaline and acidic pH. At the same time, proteolytic activity was absent in the sera-derived Ab of all healthy donors under control. Anti-histone IgGs were purified by the affinity chromatography on histone H1-Sepharose. Their cross-reactivity toward cationic proteins (histones, lysozyme, and MBP) and their capability of hydrolyzing histone H1 and MBP were detected. However, these IgGs were not cleaving core histones, lysozyme, or albumin. Capability of cleaving histone H1 and MBP was preserved after additional purification of anti-histone H1 IgGs by the HPLC gel filtration. The protease activity of anti-histone H1 IgG Ab was inhibited by serine protease inhibitors.