Amylolytic activity of IgG and sIgA immunoglobulins from human milk

Background: New natural amylolytic abzymes (Abs) for catalytically active antibodies from human milk have been identified and investigated. Methods: The amylolytic activity of human milk autoantibodies was studied by TLC and HPLC techniques analyzing the hydrolysis of maltooligosaccharides with diff...

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Bibliographic Details
Published in:Clinica chimica acta 2001-12, Vol.314 (1), p.141-152
Main Authors: Savel'ev, Andrew N, Kanyshkova, Tat'yana G, Kulminskaya, Anna A, Buneva, Valentina N, Eneyskaya, Elena V, Filatov, Michael V, Nevinsky, Georgy A, Neustroev, Kirill N
Format: Article
Language:English
Subjects:
Adult
Amylases - analysis
Amylases - metabolism
Amyloid - metabolism
Autoantibody
Chromatography, Thin Layer
Electrophoresis, Polyacrylamide Gel
Female
Glucosidases - metabolism
Human milk
Humans
Hydrolysis
Immunoblotting
Immunoglobulin A, Secretory - isolation & purification
Immunoglobulin A, Secretory - pharmacology
Immunoglobulin Fab Fragments - chemistry
Immunoglobulin Fab Fragments - isolation & purification
Immunoglobulin G - isolation & purification
Immunoglobulin G - pharmacology
Indicators and Reagents
Kinetics
Kinetics of hydrolysis of maltooligosaccharides
Maltose - chemistry
Milk, Human - enzymology
Milk, Human - immunology
Oligosaccharides - metabolism
Substrate Specificity
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Summary:Background: New natural amylolytic abzymes (Abs) for catalytically active antibodies from human milk have been identified and investigated. Methods: The amylolytic activity of human milk autoantibodies was studied by TLC and HPLC techniques analyzing the hydrolysis of maltooligosaccharides with different degrees of polymerization and of 4-nitrophenyl 4,6- O-ethylidene-α- d-maltoheptaoside (EPS). IgG and sIgA fractions were isolated from human milk by affinity chromatography. After SDS-PAGE preparation of native IgG and sIgA and their renaturation, the amylolytic activity was in-gel assayed. Results: All electrophoretically homogeneous preparations of IgG and its Fab fragments as well as sIgA antibodies possessed α-amylolytic activity. The specific activities of these catalytic antibodies varied in the range from 1.83 up to 3.33 kat/kg, which is about one order of magnitude higher than that for IgGs from the sera of cancer patients. IgG and sIgA fractions showed Michaelis constants for hydrolysis of 4-nitrophenyl 4,6- O-ethylidene-α- d-maltoheptaoside in the range of 10 −4 M/l. Fractions of autoantibodies from different donors exhibited different modes of action in hydrolysis of maltooligosaccharides, maltose and p-nitrophenyl-α- d-glucopyranose. Conclusions: IgG antibodies, their Fab fragments, and sIgA fractions isolated from human milk of healthy women possessed amylolytic activity in the hydrolysis of maltooligosaccharides and several artificial substrates.
ISSN:0009-8981
1873-3492
DOI:10.1016/S0009-8981(01)00691-X