Human autoantibodies with amylolytic activity. Ivanen, D., Kulminskaya, A., Ershova, N., Eneyskaya, E., Shabalin, K., Savel'ev, A., Kanyshkova, T., Buneva, V., Nevinsky, G., & Neustroev, K. Biologia - Section Cellular and Molecular Biology, 57(SUPPL. 11):253-260, 2002. cited By 6
Human autoantibodies with amylolytic activity [link]Paper  abstract   bibtex   
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 α-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 α-D-glucopyranoside.
@ARTICLE{Ivanen2002253,
author={Ivanen, D.R. and Kulminskaya, A.A. and Ershova, N.A. and Eneyskaya, E.V. and Shabalin, K.A. and Savel'ev, A.N. and Kanyshkova, T.G. and Buneva, V.N. and Nevinsky, G.A. and Neustroev, K.N.},
title={Human autoantibodies with amylolytic activity},
journal={Biologia - Section Cellular and Molecular Biology},
year={2002},
volume={57},
number={SUPPL. 11},
pages={253-260},
note={cited By 6},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-19044395559&partnerID=40&md5=7b3dc1b59273e9e8db00ebaa3013ce73},
affiliation={Molec. and Radiat. Biophys. Division, Petersburg Nucl. Phys. Inst. R., 188350, Gatchina, St. Petersburg, Russian Federation; Novosibirsk Inst. of Bioorg. Chem., Siberian Div. of Russ. Acad. of Sci., Novosibirsk, Russian Federation; Biophysics Department, St. Petersburg Technical University, St. Petersburg, Russian Federation},
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 α-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 α-D-glucopyranoside.},
author_keywords={α-amylase;  Autoantibodies from human;  Autoimmunity disease},
correspondence_address1={Neustroev, K.N.; Molec. and Radiat. Biophys. Division, Petersburg Nucl. Phys. Inst. R., 188350, Gatchina, St. Petersburg, Russian Federation; email: neustk@omrb.pnpi.spb.ru},
issn={13356399},
language={English},
abbrev_source_title={Biol. Sect. Cell. Mol. Biol.},
document_type={Article},
source={Scopus},
}

Downloads: 0