General Approach for Isolation of Immunoglobulins Fragments with the Core Hinge

Maria Timchenko; Vladimir Tischenko

doi:doi:10.11648/j.iji.20140203.11

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General Approach for Isolation of Immunoglobulins Fragments with the Core Hinge

Maria Timchenko, Vladimir Tischenko

Published in International Journal of Immunology (Volume 2, Issue 3)

Received: 6 October 2014 Accepted: 1 November 2014 Published: 18 November 2014

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Abstract

The original limited proteolysis approach was proposed for large (multidomain) proteins with post-translational modifications for obtaining of their novel fragments. It was realized for human immunoglobulins representing two subclasses IgG2 and IgG3. This approach was based on two techniques: masking of protein regions which are normally susceptible to proteolytic enzymes and increasing the possibility of proteolysis for sites which are not ordinarily accessible to these enzymes. The masking of immunoglobulin part which is sensitive to proteolysis was performed by Fab fragments (Fv subfragments) of antibodies and the increase of lability of stable regions was realized by pH change and mild reduction of disulfide bonds.

Published in	International Journal of Immunology (Volume 2, Issue 3)
DOI	10.11648/j.iji.20140203.11
Page(s)	16-23
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Limited Proteolysis, Immunoglobulin, Hinge, Fc Fragment, Facb Fragment

References

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Maria Timchenko, Vladimir Tischenko. (2014). General Approach for Isolation of Immunoglobulins Fragments with the Core Hinge. International Journal of Immunology, 2(3), 16-23. https://doi.org/10.11648/j.iji.20140203.11

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Maria Timchenko; Vladimir Tischenko. General Approach for Isolation of Immunoglobulins Fragments with the Core Hinge. Int. J. Immunol. 2014, 2(3), 16-23. doi: 10.11648/j.iji.20140203.11

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Maria Timchenko, Vladimir Tischenko. General Approach for Isolation of Immunoglobulins Fragments with the Core Hinge. Int J Immunol. 2014;2(3):16-23. doi: 10.11648/j.iji.20140203.11

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@article{10.11648/j.iji.20140203.11,
  author = {Maria Timchenko and Vladimir Tischenko},
  title = {General Approach for Isolation of Immunoglobulins Fragments with the Core Hinge},
  journal = {International Journal of Immunology},
  volume = {2},
  number = {3},
  pages = {16-23},
  doi = {10.11648/j.iji.20140203.11},
  url = {https://doi.org/10.11648/j.iji.20140203.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.iji.20140203.11},
  abstract = {The original limited proteolysis approach was proposed for large (multidomain) proteins with post-translational modifications for obtaining of their novel fragments. It was realized for human immunoglobulins representing two subclasses IgG2 and IgG3. This approach was based on two techniques: masking of protein regions which are normally susceptible to proteolytic enzymes and increasing the possibility of proteolysis for sites which are not ordinarily accessible to these enzymes. The masking of immunoglobulin part which is sensitive to proteolysis was performed by Fab fragments (Fv subfragments) of antibodies and the increase of lability of stable regions was realized by pH change and mild reduction of disulfide bonds.},
 year = {2014}
}

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TY  - JOUR
T1  - General Approach for Isolation of Immunoglobulins Fragments with the Core Hinge
AU  - Maria Timchenko
AU  - Vladimir Tischenko
Y1  - 2014/11/18
PY  - 2014
N1  - https://doi.org/10.11648/j.iji.20140203.11
DO  - 10.11648/j.iji.20140203.11
T2  - International Journal of Immunology
JF  - International Journal of Immunology
JO  - International Journal of Immunology
SP  - 16
EP  - 23
PB  - Science Publishing Group
SN  - 2329-1753
UR  - https://doi.org/10.11648/j.iji.20140203.11
AB  - The original limited proteolysis approach was proposed for large (multidomain) proteins with post-translational modifications for obtaining of their novel fragments. It was realized for human immunoglobulins representing two subclasses IgG2 and IgG3. This approach was based on two techniques: masking of protein regions which are normally susceptible to proteolytic enzymes and increasing the possibility of proteolysis for sites which are not ordinarily accessible to these enzymes. The masking of immunoglobulin part which is sensitive to proteolysis was performed by Fab fragments (Fv subfragments) of antibodies and the increase of lability of stable regions was realized by pH change and mild reduction of disulfide bonds.
VL  - 2
IS  - 3
ER  -

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Author Information

Maria Timchenko

Laboratory of NMR of Biosystems, Institute of Theoretical and Experimental Biophysics RAS, Pushchino, Russia
Vladimir Tischenko

Laboratory of NMR of Biosystems, Institute of Theoretical and Experimental Biophysics RAS, Pushchino, Russia

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Maria Timchenko, Vladimir Tischenko. (2014). General Approach for Isolation of Immunoglobulins Fragments with the Core Hinge. International Journal of Immunology, 2(3), 16-23. https://doi.org/10.11648/j.iji.20140203.11

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Maria Timchenko; Vladimir Tischenko. General Approach for Isolation of Immunoglobulins Fragments with the Core Hinge. Int. J. Immunol. 2014, 2(3), 16-23. doi: 10.11648/j.iji.20140203.11

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AMA Style

Maria Timchenko, Vladimir Tischenko. General Approach for Isolation of Immunoglobulins Fragments with the Core Hinge. Int J Immunol. 2014;2(3):16-23. doi: 10.11648/j.iji.20140203.11

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@article{10.11648/j.iji.20140203.11,
  author = {Maria Timchenko and Vladimir Tischenko},
  title = {General Approach for Isolation of Immunoglobulins Fragments with the Core Hinge},
  journal = {International Journal of Immunology},
  volume = {2},
  number = {3},
  pages = {16-23},
  doi = {10.11648/j.iji.20140203.11},
  url = {https://doi.org/10.11648/j.iji.20140203.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.iji.20140203.11},
  abstract = {The original limited proteolysis approach was proposed for large (multidomain) proteins with post-translational modifications for obtaining of their novel fragments. It was realized for human immunoglobulins representing two subclasses IgG2 and IgG3. This approach was based on two techniques: masking of protein regions which are normally susceptible to proteolytic enzymes and increasing the possibility of proteolysis for sites which are not ordinarily accessible to these enzymes. The masking of immunoglobulin part which is sensitive to proteolysis was performed by Fab fragments (Fv subfragments) of antibodies and the increase of lability of stable regions was realized by pH change and mild reduction of disulfide bonds.},
 year = {2014}
}

Copy | Download

TY  - JOUR
T1  - General Approach for Isolation of Immunoglobulins Fragments with the Core Hinge
AU  - Maria Timchenko
AU  - Vladimir Tischenko
Y1  - 2014/11/18
PY  - 2014
N1  - https://doi.org/10.11648/j.iji.20140203.11
DO  - 10.11648/j.iji.20140203.11
T2  - International Journal of Immunology
JF  - International Journal of Immunology
JO  - International Journal of Immunology
SP  - 16
EP  - 23
PB  - Science Publishing Group
SN  - 2329-1753
UR  - https://doi.org/10.11648/j.iji.20140203.11
AB  - The original limited proteolysis approach was proposed for large (multidomain) proteins with post-translational modifications for obtaining of their novel fragments. It was realized for human immunoglobulins representing two subclasses IgG2 and IgG3. This approach was based on two techniques: masking of protein regions which are normally susceptible to proteolytic enzymes and increasing the possibility of proteolysis for sites which are not ordinarily accessible to these enzymes. The masking of immunoglobulin part which is sensitive to proteolysis was performed by Fab fragments (Fv subfragments) of antibodies and the increase of lability of stable regions was realized by pH change and mild reduction of disulfide bonds.
VL  - 2
IS  - 3
ER  -

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