Human abzymes with amylolytic activity. Kulminskaya, A.; Saveliev, A.; and Neustroev, K. Trends in Glycoscience and Glycotechnology, 16(87):17-31, Gakushin Publishing Company, 2004. cited By 10
Human abzymes with amylolytic activity [link]Paper  doi  abstract   bibtex   
Amylolytic abzymes are a new type of catalytically active human antibodies that have been found recently. Various immunoglobulins from the sera of patients with autoimmune diseases and human milk were found to possess amylolytic activity, which is expressed in their ability to hydrolyze α-(1,4)-D- glucosyl linkages of maltooligosaccharides, starch, glycogen, and several artificial substrates. Pure IgM fractions isolated from several tens of analyzed patients with clinically definite diagnoses of multiple sclerosis (MS) and systemic lupus erythematosus (SLE) had approximately three orders of magnitude higher specific amylolytic activity than those for healthy donors. Average values for the specific amylolytic activity of IgGs and slgAs from human milk were five times less than of IgMs from autoimmune patients. Strict criteria were used to prove that the amylolytic activity of abzymes was their intrinsic property and was not due to any enzyme contamination. Fab fragments derived from IgM and IgG fractions of human abzymes displayed the same level of amylolytic activity. Values for Michaelis constants KM in the abzyme-mediated hydrolysis of different α-D-maltooligosaccharides and α-D- maltooligosaccharides with chromogenic and fluorescent label on reducing end were in the range of 1-2 to 0.01 mM. Abzyme fractions from different donors demonstrated catalytic heterogeneity in Michaelis-Menten parameters and different modes of action in the hydrolysis of natural and artificial substrates. One part of amylolytic immunoglobulins exhibited exo-amylase action when others have also α-glucosidase activity yielding glucose and capable of cleaving p-nitrophenyl α-D-glucopyranoside. Enzymatic properties of all tested amylolytic abzymes distinguished from those of putative human α-amylases. None of the IgM, IgG, and sIgA samples investigated showed transglycosylating ability.
@ARTICLE{Kulminskaya200417,
author={Kulminskaya, A.A. and Saveliev, A.N. and Neustroev, K.N.},
title={Human abzymes with amylolytic activity},
journal={Trends in Glycoscience and Glycotechnology},
year={2004},
volume={16},
number={87},
pages={17-31},
doi={10.4052/tigg.16.17},
note={cited By 10},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-1942454781&doi=10.4052%2ftigg.16.17&partnerID=40&md5=a1f5d60fa308f499596c135dbbb0648e},
affiliation={Molec. and Radiat. Biophys. Division, Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina, Russian Federation; Biophysics Department, St.-Petersburg Technical University, St. Petersburg, Russian Federation; Petersburg Nuclear Physics Institute, Russian Academy of Science, Gatchina, St. Petersburg, 188300, Russian Federation; St. Petersburg Technol. Institute, Russian Federation; Petersburg Nuclear Physics Institute, Russian Federation; Laboratory of Enzymology; Biophysics Department, St. Petersburg Polytech. University, Russian Federation; Leningrad Nuclear Physics Institute, Russian Federation},
abstract={Amylolytic abzymes are a new type of catalytically active human antibodies that have been found recently. Various immunoglobulins from the sera of patients with autoimmune diseases and human milk were found to possess amylolytic activity, which is expressed in their ability to hydrolyze α-(1,4)-D- glucosyl linkages of maltooligosaccharides, starch, glycogen, and several artificial substrates. Pure IgM fractions isolated from several tens of analyzed patients with clinically definite diagnoses of multiple sclerosis (MS) and systemic lupus erythematosus (SLE) had approximately three orders of magnitude higher specific amylolytic activity than those for healthy donors. Average values for the specific amylolytic activity of IgGs and slgAs from human milk were five times less than of IgMs from autoimmune patients. Strict criteria were used to prove that the amylolytic activity of abzymes was their intrinsic property and was not due to any enzyme contamination. Fab fragments derived from IgM and IgG fractions of human abzymes displayed the same level of amylolytic activity. Values for Michaelis constants KM in the abzyme-mediated hydrolysis of different α-D-maltooligosaccharides and α-D- maltooligosaccharides with chromogenic and fluorescent label on reducing end were in the range of 1-2 to 0.01 mM. Abzyme fractions from different donors demonstrated catalytic heterogeneity in Michaelis-Menten parameters and different modes of action in the hydrolysis of natural and artificial substrates. One part of amylolytic immunoglobulins exhibited exo-amylase action when others have also α-glucosidase activity yielding glucose and capable of cleaving p-nitrophenyl α-D-glucopyranoside. Enzymatic properties of all tested amylolytic abzymes distinguished from those of putative human α-amylases. None of the IgM, IgG, and sIgA samples investigated showed transglycosylating ability.},
author_keywords={Abzymes;  Amylolytic activity;  Autoimmune pothotogies},
correspondence_address1={Neustroev, K.N.; Petersburg Nuclear Physics Institute, Russian Academy of Science, Gatchina, St. Petersburg, 188300, Russian Federation; email: neustk@omrb.pnpi.spb.ru},
publisher={Gakushin Publishing Company},
issn={09157352},
language={English; Japanese},
abbrev_source_title={Trends Glycosci. Glycotechnol.},
document_type={Short Survey},
source={Scopus},
}
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