Biologia, Bratislava, 57/Suppl. 11: 253-260, 2002.

ISSN 0006-3088 (Biologia).

 

Full Paper

Human autoantibodies with amylolytic activity.

 

Dina R. Ivanen1, Anna A. Kulminskaya1, Nadezhda A. Ershova2, Elena V. Eneyskaya1, Konstantin A. Shabalin1, Andrew N. Savelev3, Tatyana G. Kanyshkova2, Valentina N. Buneva2, Georgy A. Nevinsky2 & Kirill N. Neustroev1*

1 Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute of Russian Academy of Sciences, 188350, Gatchina, St. Petersburg, Russia; tel.: ++ 7 81271 32014, fax: ++ 7 81271 32303, e-mail: neustk@omrb.pnpi.spb.ru

2 Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of Russian Academy of Sciences, Novosibirsk, Russia

3 Biophysics Department, St. Petersburg Technical University, St. Petersburg, Russia

* corresponding author

Received: October 4, 2001 / Accepted: February 12, 2002

 

Abstract

We have investigated the activity of IgG and IgM fractions from patients suffering from multiple sclerosis, as well as that of IgG and sIgA fractions isolated from human milk of healthy women, in the hydrolysis of artificial substrates and maltooligosaccharides with different degrees of polymerisation. All electrophoretically-homogeneous preparations of IgG and its Fab fragments, as well as sIgA and IgM antibodies, possessed amylolytic activity. The specific activities of catalytic antibodies from human milk varied in the range from 0.11 up to 0.2 U/mg, i.e. about three orders higher than those for IgGs from the sera of multiple sclerosis patients and one order higher than those for cancer patients. Milk IgG and sIgA fractions revealed Michaelis constants for hydrolysis of p-nitrophenyl a-D-maltooligosides in the range of 10-4 M. Fractions of autoantibodies from various donors revealed different modes of action in hydrolysis of maltooligosaccharides, p-nitrophenyl maltooligosaccharides and p-nitrophenyl a-D-glucopyranoside.

 

Key words: autoantibodies from human, a-amylase, autoimmunity disease.