Literature DB >> 17140382

Polysaccharide kinase activity of human milk IgG antibodies.

N A Karataeva1, V N Buneva, G A Nevinsky.   

Abstract

A small fraction of human milk IgG antibodies is shown to possess polysaccharide kinase activity for the first time. Unlike all known kinases, IgG antibodies can use as phosphate donor not only [gamma-(32)P]ATP, but also directly [(32)P]ortho-phosphate. Human milk IgGs therefore possess high affinity to ortho-phosphate (K(m) = 9-71 microM), which is a more effective substrate than ATP. IgG antibodies possessing polysaccharide kinase activity are yet another example of natural abzymes possessing not hydrolytic, but synthetic enzymatic activity.

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Year:  2006        PMID: 17140382     DOI: 10.1134/s000629790611006x

Source DB:  PubMed          Journal:  Biochemistry (Mosc)        ISSN: 0006-2979            Impact factor:   2.487


  3 in total

1.  IgGs from Human Milk Hydrolyze microRNAs.

Authors:  Ivan Yu Kompaneets; Evgeny A Ermakov; Sergey E Sedykh; Valentina N Buneva; Georgy A Nevinsky
Journal:  Molecules       Date:  2020-05-20       Impact factor: 4.411

2.  Human milk IgGs contain various combinations of different antigen-binding sites resulting in multiple variants of their bispecificity.

Authors:  Sergey E Sedykh; Valentina N Buneva; Georgy A Nevinsky
Journal:  PLoS One       Date:  2012-08-13       Impact factor: 3.240

3.  Human milk sIgA molecules contain various combinations of different antigen-binding sites resulting in a multiple binding specificity of antibodies and enzymatic activities of abzymes.

Authors:  Sergey E Sedykh; Valentina N Buneva; Georgy A Nevinsky
Journal:  PLoS One       Date:  2012-11-02       Impact factor: 3.240

  3 in total

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